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Total number of results for Bos taurus are 192
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NPID Sequence Length Organism Family Name PMID Peptide_REF
NP00021
MSLQADFDKAAKDVRKLKTRPDDEELKELYGLYKQSVIGDIDIECPALLDLKGKAKWEAWNLQKGLSKEDAMNAYISKAKELIEKYGI
88 Bos taurus ACBP Acyl-CoA-binding domain-containing protein 7
NP00022
MCQVEFEMACAAIKQLKGPVSDQEKLLVYSYYKQATQGDCNIPAPPATDLKAKAKWEAWNENKGMSKMDAMRIYIAKVEELKKNEAG
87 Bos taurus ACBP Diazepam-binding inhibitor-like 5
NP00033
SQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI
86 Bos taurus ACBP Acyl-CoA-binding protein 3525533# Marquardt H., Todaro G.J., Shoyab M.; # "Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor."; # J. Biol. Chem. 261:9727-9731(1986).$3663196#Mikkelsen J., Hoejrup P., Nielsen P.F., Roepstorff P., Knudsen J.; #"Amino acid sequence of acyl-CoA-binding protein from cow liver."; #Biochem. J. 245:857-861(1987).$1622397#Jensen M.S., Hoejrup P., Rasmussen J.T., Knudsen J.; #"Purification and characterization of variants of acyl-CoA-binding protein in the bovine liver."; #Biochem. J. 284:809-812(1992).
NP00039
YRQSLNNFQGLRSFGCRFGTCTVQKLAHQIYHFTDKDKDGSAPRSKISPQGY
52 Bos taurus Adrenomedullin Adrenomedullin
NP00040
LRSFGCRFGTCTVQKL
16 Bos taurus Adrenomedullin Adrenomedullin-11-26
NP00041
ARLDVAAEFRKKWNKWALSR
20 Bos taurus Adrenomedullin Proadrenomedullin N-20 terminal peptide
NP00597
QRPRLSHKGPMPF
13 Bos taurus Apelin Apelin-13
NP00598
SGPGPWQGGRRKFRRQRPRLSHKGPMPF
28 Bos taurus Apelin Apelin-28
NP00599
GPRSGPGPWQGGRRKFRRQRPRLSHKGPMPF
31 Bos taurus Apelin Apelin-31
NP00600
LVQPRGPRSGPGPWQGGRRKFRRQRPRLSHKGPMPF
36 Bos taurus Apelin Apelin-36
NP00786
APVTAGRGGALAKMYTRGNHWAVGHLM
27 Bos taurus Bombesin/neuromedin-B/ranatensin Gastrin-releasing peptide
NP00787
GNHWAVGHLM
10 Bos taurus Bombesin/neuromedin-B/ranatensin Neuromedin-C 2755876# Lemaire S., Trifaro J.-M., Chouinard L., Cecyre D., Dessureault J., Mercier P., Dumont M.; # "Structural identification, subcellular localization and secretion of bovine adrenomedullary neuromedin C [GRP-(18-27)]."; # Peptides 10:355-360(1989).
NP00788
GNLWATGHFM
10 Bos taurus Bombesin/neuromedin-B/ranatensin Neuromedin-B
NP00789
APLGWDLPESRSRASKIRVHPRGNLWATGHFM
32 Bos taurus Bombesin/neuromedin-B/ranatensin Neuromedin-B-32
NP00809
KRPPGFSPFR
10 Bos taurus Bradykinin Lysyl-bradykinin 4986212#Kato H., Nagasawa S., Suzuki T.#Studies on the structure of bovine kininogen: cleavages of disulfide bonds and of methionyl bonds in kininogen-II.#J. Biochem. 67:313-323(1970).
NP00810
RPPGFSPFR
9 Bos taurus Bradykinin Bradykinin 4986212#Kato H., Nagasawa S., Suzuki T.#Studies on the structure of bovine kininogen: cleavages of disulfide bonds and of methionyl bonds in kininogen-II.#J. Biochem. 67:313-323(1970).
NP00820
ACNTATCMTHRLAGWLSRSGSMVRSNLLPTKMGFKIFNGPRRNSWF
46 Bos taurus Calcitonin Calcitonin receptor-stimulating peptide 1
NP00844
CSNLSTCVLSAYWKDLNNYHRFSGMGFGPETP
32 Bos taurus Calcitonin Calcitonin 5259773# Brewer H.B. Jr., Ronan R.; # "Amino acid sequence of bovine thyrocalcitonin."; # Proc. Natl. Acad. Sci. U.S.A. 63:940-947(1969).
NP00845
CGTATCETQRLANFLAPSSNKLGAIFSPTKMGSNTY
36 Bos taurus Calcitonin Islet amyloid polypeptide
NP00867
QEDAELQPRALDIYSAVEDASHEKELIEALQEVLKKLKS
39 Bos taurus CART CART(1-39) (By similarity)
NP00868
IPIYEKKYGQVPMCDAGEQCAVRKGARIGKLCDCPRGTSCNSFLLKCL
48 Bos taurus CART CART(42-89) (By similarity)
NP00880
QEDAELQPRALDIYSAVEDASHEKELIEALQEVLKKLKSKRIPIYEKKYGQVPMCDAGEQCAVRKGARIGKLCDCPRGTSCNSFLLKCL
89 Bos taurus CART Cocaine- and amphetamine-regulated
NP00905
GSAKVAFSAIRSTNH
15 Bos taurus Cerebellins [des-Ser1]-cerebellin (Potential)
NP00906
SGSAKVAFSAIRSTNH
16 Bos taurus Cerebellins Cerebellin #Colgrave M.;#"Neuropeptidomics of the bovine hypothalamus.";# Submitted (JAN-2010) to UniProtKB.
NP00907
QNETEPIVLEGKCLVVCDSNPTSDPTGTALGISVRSGSAKVAFSAIRSTNHEPSEMSNRTMIIYFDQVLVNIGNNFDSERSTFIAPRKGIYSFNFHVVKVYNRQTIQVSLMLNGWPVISAFAGDQDVTREAASNGVLIQMEKGDRAYLKLERGNLMGGWKYSTFSGFLVFPL
172 Bos taurus Cerebellins Cerebellin-1
NP00908
QEGTEPVLLEGECLVVCEPGRAAAGGPGGAALGEAPPGRVAFAAVRSHHHEPAGEIGNGTSGAIYFDQVLVNEGGGFDRTSGSFVAPVRGVYSFRFHVVKVYNRQTVQVSLMLNTWPVVSAFANDPDVTREAATSSVLLPLDPGDRVSLRLRRGNLLGGWKYSSFSGFLIFPL
173 Bos taurus Cerebellins Cerebellin-3
NP00945
FPKPAGSQDKPLHNRELSAERPLNEQIAEAEADEIKKTYPPENKPGESNYSFVDNLNLLKAITEKEKNEKERQSVKISPNDNKLNVEDVDSTKNRRLIDDYDSTKSGLDRKFQDDPDGLHQLDGTPLTAEDIVQKIATRIYEENDRGVFDRIVSKLLNLGLITESQAHTLEDEVAEVLQKLISKEANNYEEELNKPTSKTESQTGKIPEKVTPMAAIQDAFTNGENDETVSNTLTLTNGLERRTKTYSEDNFEELQYFPNFYALLKSIDSEKEAKEKETLITIMKTLIDFVKMMVKYGTISPEEGVSYLENLDETIALQTKNKLEKNVTDNKSKLFAVPSEKSHEETDSTKEEAAKMEKEYGTLKDSTKDDDSNPRGKTDEHKGKTEAYLEAIRKNIDWLKKHNKKENKEDYDLSKMRDFINQQADAYVEKGILDKEEADAIKRIYSSL
449 Bos taurus Chromogranin/secretogranin Secretogranin-3
NP00969
RSMRLSFRARGYGFRGPGLQL
21 Bos taurus Chromogranin/secretogranin Catestatin 12795588# Lee J.C., Taylor C.V., Gaucher S.P., Toneff T., Taupenot L., Yasothornsrikul S., Mahata S.K., Sei C., Parmer R.J., Neveu J.M., Lane W.S., Gibson B.W., O'Connor D.T., Hook V.Y.H.; # "Primary sequence characterization of catestatin intermediates and peptides defines proteolytic cleavage sites utilized for converting chromogranin A into active catestatin secreted from neuroendocrine chromaffin cells."; # Biochemistry 42:6938-6946(2003).$9786174#Kennedy BP, Mahata SK, O'Connor DT, Ziegler MG#Mechanism of cardiovascular actions of the chromogranin A fragment catestatin in vivo#Peptides 1998;19(7):1241-8
NP00970
YPGPQAKEDSEGPSQGPASREK
22 Bos taurus Chromogranin/secretogranin Chromacin 8910482#Strub J.-M., Goumon Y., Lugardon K., Capon C., Lopez M., Moniatte M., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.; #"Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules."; #J. Biol. Chem. 271:28533-28540(1996).
NP00971
LPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKYPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKPPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGKSGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEKRLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLEELRRG
431 Bos taurus Chromogranin/secretogranin Chromogranin-A
NP00972
SDEDSDGDRPQASPGLGPGP
20 Bos taurus Chromogranin/secretogranin Chromostatin 1996343#Galindo E., Rill A., Bader M.-F., Aunis D.; #"Chromostatin, a 20-amino acid peptide derived from chromogranin A, inhibits chromaffin cell secretion."; #Proc. Natl. Acad. Sci. U.S.A. 88:1426-1430(1991).
NP00973
AAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRG
47 Bos taurus Chromogranin/secretogranin Pancreastatin 2756155#Nakano I., Funakoshi A., Miyasaka K., Ishida K., Makk G., Angwin P., Chang D., Tatemoto K.; #"Isolation and characterization of bovine pancreastatin."; #Regul. Pept. 25:207-213(1989).
NP00974
LPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQ
76 Bos taurus Chromogranin/secretogranin Vasostatin-1 12795588# Lee J.C., Taylor C.V., Gaucher S.P., Toneff T., Taupenot L., Yasothornsrikul S., Mahata S.K., Sei C., Parmer R.J., Neveu J.M., Lane W.S., Gibson B.W., O'Connor D.T., Hook V.Y.H.; # "Primary sequence characterization of catestatin intermediates and peptides defines proteolytic cleavage sites utilized for converting chromogranin A into active catestatin secreted from neuroendocrine chromaffin cells."; # Biochemistry 42:6938-6946(2003).
NP00975
WSKMDQLAKELTAE
14 Bos taurus Chromogranin/secretogranin WE-14
NP00976
SAEFPDFYDSEEQMSPQHTAENEEEKAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGTRRG
63 Bos taurus Chromogranin/secretogranin CCB peptide 15174145#Gasnier C., Lugardon K., Ruh O., Strub J.-M., Aunis D., Metz-Boutigue M.H.; #"Characterization and location of post-translational modifications on chromogranin B from bovine adrenal medullary chromaffin granules."; #Proteomics 4:1789-1801(2004).
NP00977
QYDRVAELDQLLHY
14 Bos taurus Chromogranin/secretogranin Peptide BAM-1745 1554736#Dillen L., Boel S., De Potter W.P., Claeys M.; #"Mass spectrometric characterization of bovine chromaffin granule peptides related to chromogranin B."; #Biochim. Biophys. Acta 1120:105-112(1992).$1982622#Flanagan T., Taylor L., Poulter L., Viveros O.H., Diliberto E.J. Jr.; #"A novel 1745-dalton pyroglutamyl peptide derived from chromogranin B is in the bovine adrenomedullary chromaffin vesicle."; #Cell. Mol. Neurobiol. 10:507-523(1990).$15174145#Gasnier C., Lugardon K., Ruh O., Strub J.-M., Aunis D., Metz-Boutigue M.H.; #"Characterization and location of post-translational modifications on chromogranin B from bovine adrenal medullary chromaffin granules."; #Proteomics 4:1789-1801(2004).
NP00978
MPVDIRNHNEEVVTHCIIEVLSNALLKSSAPPITPECRQVLKKNGKELKNEEKSENENTRFEVRLLRDPADTSEAPGLSSREDSGEGDAQVPTVADTESGGHSRERAGEPPGSQVAKEAKTRYSKSEGQNREEEMVKYQKRERGEVGSEERLSEGPGKAQTAFLNQRNQTPAKKEELVSRYDTQSARGLEKSHSRERSSQESGEETKSQENWPQELQRHPEGQEAPGESEEDASPEVDKRHSRPRHHHGRSRPDRSSQEGNPPLEEESHVGTGNSDEEKARHPAHFRALEEGAEYGEEVRRHSAAQAPGDLQGARFGGRGRGEHQALRRPSEESLEQENKRHGLSPDLNMAQGYSEESEEERGPAPGPSYRARGGEAAAYSTLGQTDEKRFLGETHHRVQESQRDKARRRLPGELRNYLDYGEEKGEEAARGKWQPQGDPRDADENREEARLRGKQYAPHHITEKRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGEEENGLTLNEKNFFPEYNYDWWEKKPFEEDVNWGYEKRNPVPKLDLKRQYDRVAELDQLLHYRKKSAEFPDFYDSEEQMSPQHTAENEEEKAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGTRRG
626 Bos taurus Chromogranin/secretogranin Secretogranin-1
NP00979
QYAPHHITEKRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGEEENGLTLNEKNFFPEYNYDWWEKKPFEEDVNWGYEKRNPVPKLDLKR
91 Bos taurus Chromogranin/secretogranin Secretogranin-1(476-566)
NP00980
QKIAEKFSGTRRG
13 Bos taurus Chromogranin/secretogranin Secretolytin 7744058#Strub J.-M., Garcia-Sablone P., Lonning K., Taupenot L., Hubert P., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.; #"Processing of chromogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity."; #Eur. J. Biochem. 229:356-368(1995).
NP00981
QRNQLLQKEPDLRLENVQRFPSPEMIRALEYIEKLRQQAHKEESSPDYNPYQGVSVPLQQKENGDLPESSRDSLSEDEWMKIIAEALRQAENEPQSAPKENKPYTLNSEKNFPMDMPDDYETQQWAERKLKHMRFPPMYEENSRDNPFKRTNEIVEEQYTPQNLATLESVFQELGKLTGPNSQKRERADEEQKLYTDDEDDIYKANNIAYEDVVGGEDWNPVEEKIESQTQEEVRDSKENADKTEQINDEMKRSGQLGLQDEDLRKESKDQLSDDVSKVITYLKRLVNAAGSGRSQNGQTGERAIRLFEKPLDPQSIYQLIEISRNLQIPPEDLIDMLKTGEKPVEPEQELEIPVEPEDISEVDLDHPDLFQNKMLSKNGYPKAPGHAVAEALSEGLSVEDILNLLGMESAANPKPPYFPNQYNREKVLSRLPYGPGRSKANQLPKAVWMPDVENRQMAYENLNDKDQELGEYLARMLVKYPEIMNANPAKRVPSQGSTEDDRQDENQIEQALKEHLSQHSSQETDKLASVSKRLPVGTPKSDDTPNRPYLDEDLLVKVLEYLNQEKAEKGREHIAKRAMENM
583 Bos taurus Chromogranin/secretogranin Secretogranin-2
NP00982
TNEIVEEQYTPQNLATLESVFQELGKLTGPNSQ
33 Bos taurus Chromogranin/secretogranin Secretoneurin
NP01085
QESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGECTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQRQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPVKDFVQPPTRLCAGCPKPIPVDSPDLEEPLSHSIAKLNAEHDGAFYFKIDTVKKATVQVVAGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWEEKVYPTVNCQPLGQTSLMKRPPGFSPFRSVQVMKTEGSTTVSLPHSAMSPVQDEERDSGKEQGPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHGSHGLGHGHQKQHGLGHGHKHGHGHGKHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDFQDSDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVNGVNPTVEMKESHDFDLVDALL
603 Bos taurus Cystatin Kininogen-1 3546295#Sueyoshi T., Miyata T., Hashimoto N., Kato H., Hayashida H., Miyata T., Iwanaga S.#Bovine high molecular weight kininogen. The amino acid sequence, positions of carbohydrate chains and disulfide bridges in the heavy chain portion.# J. Biol. Chem. 262:2768-2779(1987).$4986212#Kato H., Nagasawa S., Suzuki T.#Studies on the structure of bovine kininogen: cleavages of disulfide bonds and of methionyl bonds in kininogen-II.#J. Biochem. 67:313-323(1970).$1169237#Han Y.N., Komiya M., Iwanaga S., Suzuki T.#Studies on the primary structure of bovine high-molecular-weight kininogen. Amino acid sequence of a fragment ('histidine-rich peptide') released by plasma kallikrein.#J. Biochem. 77:55-68(1975).
NP01086
QESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGECTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQRQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPVKDFVQPPTRLCAGCPKPIPVDSPDLEEPLSHSIAKLNAEHDGAFYFKIDTVKKATVQVVAGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWEEKVYPTVNCQPLGQTSLM
360 Bos taurus Cystatin Kininogen-1 heavy chain 3546295#Sueyoshi T., Miyata T., Hashimoto N., Kato H., Hayashida H., Miyata T., Iwanaga S.#Bovine high molecular weight kininogen. The amino acid sequence, positions of carbohydrate chains and disulfide bridges in the heavy chain portion.# J. Biol. Chem. 262:2768-2779(1987).
NP01087
SVQVMKTEGSTTVSLPHSAMSPVQDEERDSGKEQGPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHGSHGLGHGHQKQHGLGHGHKHGHGHGKHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDFQDSDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVNGVNPTVEMKESHDFDLVDALL
233 Bos taurus Cystatin Kininogen-1 light chain 1169237#Han Y.N., Komiya M., Iwanaga S., Suzuki T.#Studies on the primary structure of bovine high-molecular-weight kininogen. Amino acid sequence of a fragment ('histidine-rich peptide') released by plasma kallikrein.#J. Biochem. 77:55-68(1975).
NP01088
QESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGQCTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQKQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPGEDFLPPMVCVGCPKPIPVDSPDLEEALNHSIAKLNAEHDGTFYFKIDTVKKATVQVVGGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWEEKVYPTVNCQPLGQTSLMKRPPGFSPFRSVQVMKTEGSTTVSLPHSAMSPVQDEERDSGKEQGPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHRSHGLGHGHQKQHGLGHGHKHGHGHGKHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDFQDSDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVNGVNPTVEMKESHDFDLVDALL
601 Bos taurus Cystatin Kininogen-2 3546295#Sueyoshi T., Miyata T., Hashimoto N., Kato H., Hayashida H., Miyata T., Iwanaga S.#Bovine high molecular weight kininogen. The amino acid sequence, positions of carbohydrate chains and disulfide bridges in the heavy chain portion.# J. Biol. Chem. 262:2768-2779(1987).$4986212#Kato H., Nagasawa S., Suzuki T.#Studies on the structure of bovine kininogen: cleavages of disulfide bonds and of methionyl bonds in kininogen-II.#J. Biochem. 67:313-323(1970).$956151#Han Y.N., Kato H., Iwanaga S., Suzuki T.#Primary structure of bovine plasma high-molecular-weight kininogen. The amino acid sequence of a glycopeptide portion (fragment 1) following the C-terminus ot the bradykinin moiety.#J. Biochem. 79:1201-1222(1976).$1169237#Han Y.N., Komiya M., Iwanaga S., Suzuki T.#Studies on the primary structure of bovine high-molecular-weight kininogen. Amino acid sequence of a fragment ('histidine-rich peptide') released by plasma kallikrein.#J. Biochem. 77:55-68(1975).
NP01089
QESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGQCTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQKQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPGEDFLPPMVCVGCPKPIPVDSPDLEEALNHSIAKLNAEHDGTFYFKIDTVKKATVQVVGGLKYSIVFIARETTCSKGSNEELTKSCEINIHGQILHCDANVYVVPWEEKVYPTVNCQPLGQTSLM
358 Bos taurus Cystatin Kininogen-2 heavy chain 3546295#Sueyoshi T., Miyata T., Hashimoto N., Kato H., Hayashida H., Miyata T., Iwanaga S.#Bovine high molecular weight kininogen. The amino acid sequence, positions of carbohydrate chains and disulfide bridges in the heavy chain portion.# J. Biol. Chem. 262:2768-2779(1987).
NP01090
SVQVMKTEGSTTVSLPHSAMSPVQDEERDSGKEQGPTHGHGWDHGKQIKLHGLGLGHKHKHDQGHGHHRSHGLGHGHQKQHGLGHGHKHGHGHGKHKNKGKNNGKHYDWRTPYLASSYEDSTTSSAQTQEKTEETTLSSLAQPGVAITFPDFQDSDLIATVMPNTLPPHTESDDDWIPDIQTEPNSLAFKLISDFPETTSPKCPSRPWKPVNGVNPTVEMKESHDFDLVDALL
233 Bos taurus Cystatin Kininogen-2 light chain 956151#Han Y.N., Kato H., Iwanaga S., Suzuki T.#Primary structure of bovine plasma high-molecular-weight kininogen. The amino acid sequence of a glycopeptide portion (fragment 1) following the C-terminus ot the bradykinin moiety.#J. Biochem. 79:1201-1222(1976).$1169237#Han Y.N., Komiya M., Iwanaga S., Suzuki T.#Studies on the primary structure of bovine high-molecular-weight kininogen. Amino acid sequence of a fragment ('histidine-rich peptide') released by plasma kallikrein.#J. Biochem. 77:55-68(1975).
NP01116
CSCSSLMDKECVYFCHLDIIW
21 Bos taurus Endothelin/sarafotoxin Endothelin-1
NP01117
CSCSSWLDKECVYFCHLDIIW
21 Bos taurus Endothelin/sarafotoxin Endothelin-2
NP01610
AGEGLSSPFWSLAAPQRF
18 Bos taurus FMRFamide related peptide Neuropeptide AF
NP01611
FLFQPQRF
8 Bos taurus FMRFamide related peptide Neuropeptide FF
NP01612
SPAFLFQPQRF
11 Bos taurus FMRFamide related peptide Neuropeptide SF
NP01613
SLTFEEVKDWAPKIKMNKPVVNKMPPSAANLPLRF
35 Bos taurus FMRFamide related peptide Neuropeptide NPSF 11583817#Fukusumi S., Habata Y., Yoshida H., Iijima N., Kawamata Y., Hosoya M., Fujii R., Hinuma S., Kitada C., Shintani Y., Suenaga M., Onda H., Nishimura O., Tanaka M., Ibata Y., Fujino M.; #Characteristics and distribution of endogenous RFamide-related peptide-1.; #Biochim. Biophys. Acta 1540:221-232(2001).
NP01614
WVPNLPQRF
9 Bos taurus FMRFamide related peptide Neuropeptide NPVF (By similarity)
NP01615
MPPSAANLPLRF
12 Bos taurus FMRFamide related peptide Neuropeptide RFRP-1 (Potential)
NP01616
STRAMAHLPLRL
12 Bos taurus FMRFamide related peptide Neuropeptide RFRP-2 (Potential)
NP02005
TPDINPAWYAGRGIRPVGRF
20 Bos taurus FMRFamide related peptide Prolactin-releasing peptide PrRP20
NP02006
SRAHQHSMEIRTPDINPAWYAGRGIRPVGRF
31 Bos taurus FMRFamide related peptide Prolactin-releasing peptide PrRP31
NP02020
GWTLNSAGYLLGPHALDSHRSFQDKHGLA
29 Bos taurus Galanin Galanin
NP02021
ELEPEDEARPGSFDRPLAENNVVRTIIEFLTFLHLKDAGALERLPSLPTAESAEDAERS
59 Bos taurus Galanin Galanin message-associated peptide
NP02229
QPMPHADPTGPRAQQAEEAPRRQLRAVPRVDDEPRAQLGALLARYIQQARKAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDFGRRSAEEFEYTS
95 Bos taurus Gastrin/cholecystokinin Cholecystokinin
NP02230
ISDRDYMGWMDF
12 Bos taurus Gastrin/cholecystokinin Cholecystokinin-12
NP02231
LDPSHRISDRDYMGWMDF
18 Bos taurus Gastrin/cholecystokinin Cholecystokinin-18 (By similarity)
NP02232
VIKNLQSLDPSHRISDRDYMGWMDF
25 Bos taurus Gastrin/cholecystokinin Cholecystokinin-25 (By similarity)
NP02233
KAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDF
33 Bos taurus Gastrin/cholecystokinin Cholecystokinin-33
NP02234
YIQQARKAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDF
39 Bos taurus Gastrin/cholecystokinin Cholecystokinin-39 4011954#Carlquist M., Mutt V., Joernvall H.; #"Characterization of two novel forms of cholecystokinin isolated from bovine upper intestine."; #Regul. Pept. 11:27-34(1985).
NP02235
GWMDF
5 Bos taurus Gastrin/cholecystokinin Cholecystokinin-5 (By similarity)
NP02236
AVPRVDDEPRAQLGALLARYIQQARKAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDF
58 Bos taurus Gastrin/cholecystokinin Cholecystokinin-58
NP02237
AVPRVDDEPRAQLGALLARYIQQARKAPSGRMSVIKNLQSLDPSHRISD
49 Bos taurus Gastrin/cholecystokinin Cholecystokinin-58 desnonopeptide (By similarity)
NP02238
YMGWMDF
7 Bos taurus Gastrin/cholecystokinin Cholecystokinin-7 (By similarity)
NP02239
DYMGWMDF
8 Bos taurus Gastrin/cholecystokinin Cholecystokinin-8
NP02240
QLGLQDPPHMVADLSKKQGPWVEEEEAAYGWMDF
34 Bos taurus Gastrin/cholecystokinin Big gastrin
NP02241
QGPWVEEEEAAYGWMDF
17 Bos taurus Gastrin/cholecystokinin Gastrin 5665711# Agarwal K.L., Beacham J., Bentley P.H., Gregory R.A., Kenner G.W., Sheppard R.C., Tracy H.J.; # "Isolation, structure and synthesis of ovine and bovine gastrins."; # Nature 219:614-615(1968).
NP02274
YADAIFTNSYRKVLGQLSARKLLQDIMNRQQGERNQGAKVRL
42 Bos taurus Glucagon</