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PRL_BOVIN
ID   PRL_BOVIN               Reviewed;         229 AA.
AC   P01239; A6QLX8; Q29417; Q95112;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Prolactin;
DE            Short=PRL;
DE   Flags: Precursor;
GN   Name=PRL;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6274859; DOI=10.1016/s0021-9258(19)68247-5;
RA   Sasavage N.L., Nilson J.H., Horowitz S., Rottman F.M.;
RT   "Nucleotide sequence of bovine prolactin messenger RNA. Evidence for
RT   sequence polymorphism.";
RL   J. Biol. Chem. 257:678-681(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=12561222;
RA   Cao X., Wang Q., Yan J.B., Yang F.K., Huang S.Z., Zeng Y.T.;
RT   "Molecular cloning and analysis of bovine prolactin full-long genomic as
RT   well as cDNA sequences.";
RL   Yi Chuan Xue Bao 29:768-773(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal medulla;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-68 AND 96-229.
RA   Rubtsov P.M., Oganesyan R.G., Gorbulev V.G., Skryabin K.G., Baev A.A.;
RT   "Genetic engineering of peptide hormones. II. Possible polymorphism of
RT   preprolactin in cattle. Data of molecular cloning.";
RL   Mol. Biol. (Mosk.) 22:117-127(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RX   PubMed=6086257; DOI=10.1089/dna.1.1984.3.237;
RA   Camper S.A., Luck D.N., Yao Y., Woychik R.P., Goodwin R.G., Lyons R.H.,
RA   Rottman F.M.;
RT   "Characterization of the bovine prolactin gene.";
RL   DNA 3:237-249(1984).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-229.
RX   PubMed=6299665; DOI=10.1089/dna.1.1981.1.37;
RA   Miller W.L., Coit D., Baxter J.D., Martial J.A.;
RT   "Cloning of bovine prolactin cDNA and evolutionary implications of its
RT   sequence.";
RL   DNA 1:37-50(1981).
RN   [7]
RP   SEQUENCE REVISION.
RX   PubMed=6897772; DOI=10.1089/dna.1.1982.1.313;
RA   Miller W.L., Coit D., Baxter J.D., Martial J.A.;
RT   "Bovine prolactin: corrected cDNA sequence and genetic polymorphisms.";
RL   DNA 1:313-314(1982).
RN   [8]
RP   PRELIMINARY PROTEIN SEQUENCE OF 31-229.
RX   PubMed=4608931; DOI=10.1016/0014-5793(74)80726-x;
RA   Wallis M.;
RT   "The primary structure of bovine prolactin.";
RL   FEBS Lett. 44:205-208(1974).
RN   [9]
RP   PROTEIN SEQUENCE OF 31-46.
RX   PubMed=5507606;
RA   Graf L., Cseh G., Nagy I., Kurcz M.;
RT   "An evidence for deamidation of prolactin monomer.";
RL   Acta Biochim. Biophys. Acad. Sci. Hung. 5:299-303(1970).
RN   [10]
RP   PROTEIN SEQUENCE OF 52-72 AND 120-133, AND PHOSPHORYLATION AT SER-56;
RP   SER-64 AND SER-120.
RC   TISSUE=Pituitary;
RX   PubMed=8250856; DOI=10.1042/bj2960041;
RA   Kim B.G., Brooks C.L.;
RT   "Isolation and characterization of phosphorylated bovine prolactin.";
RL   Biochem. J. 296:41-47(1993).
CC   -!- FUNCTION: Prolactin acts primarily on the mammary gland by promoting
CC       lactation.
CC   -!- SUBUNIT: Interacts with PRLR. {ECO:0000250|UniProtKB:P01236}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
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DR   EMBL; V00112; CAA23446.1; -; mRNA.
DR   EMBL; BC148124; AAI48125.1; -; mRNA.
DR   EMBL; AF426315; AAL28075.1; -; Genomic_DNA.
DR   EMBL; M36873; AAA30737.1; -; mRNA.
DR   EMBL; M36874; AAA30738.1; -; mRNA.
DR   EMBL; X14320; CAA32500.1; -; mRNA.
DR   EMBL; X14321; CAA32501.1; -; mRNA.
DR   EMBL; X01452; CAB57794.1; -; Genomic_DNA.
DR   EMBL; X01744; CAA25880.1; -; Genomic_DNA.
DR   PIR; A92378; LCBO.
DR   RefSeq; NP_776378.2; NM_173953.2.
DR   PDB; 3JC2; EM; 3.60 A; w=12-30.
DR   PDBsum; 3JC2; -.
DR   AlphaFoldDB; P01239; -.
DR   SMR; P01239; -.
DR   STRING; 9913.ENSBTAP00000020313; -.
DR   iPTMnet; P01239; -.
DR   PaxDb; P01239; -.
DR   Ensembl; ENSBTAT00000020313; ENSBTAP00000020313; ENSBTAG00000015274.
DR   GeneID; 280901; -.
DR   KEGG; bta:280901; -.
DR   CTD; 5617; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015274; -.
DR   eggNOG; ENOG502QYU3; Eukaryota.
DR   GeneTree; ENSGT00950000182818; -.
DR   HOGENOM; CLU_088274_0_1_1; -.
DR   InParanoid; P01239; -.
DR   OMA; NEVYSRW; -.
DR   OrthoDB; 1290070at2759; -.
DR   TreeFam; TF332592; -.
DR   Reactome; R-BTA-1170546; Prolactin receptor signaling.
DR   Reactome; R-BTA-982772; Growth hormone receptor signaling.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000015274; Expressed in adenohypophysis and 60 other tissues.
DR   ExpressionAtlas; P01239; baseline.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR   GO; GO:0005148; F:prolactin receptor binding; ISS:AgBase.
DR   GO; GO:0009058; P:biosynthetic process; IDA:AgBase.
DR   GO; GO:0001825; P:blastocyst formation; IDA:AgBase.
DR   GO; GO:0007565; P:female pregnancy; IBA:GO_Central.
DR   GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
DR   GO; GO:0048571; P:long-day photoperiodism; IDA:AgBase.
DR   GO; GO:0030879; P:mammary gland development; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:AgBase.
DR   GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IMP:AgBase.
DR   GO; GO:0030072; P:peptide hormone secretion; ISS:AgBase.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IMP:AgBase.
DR   GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISS:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
DR   GO; GO:1903489; P:positive regulation of lactation; IMP:AgBase.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:AgBase.
DR   GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:AgBase.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:AgBase.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IDA:AgBase.
DR   GO; GO:0043207; P:response to external biotic stimulus; IDA:AgBase.
DR   GO; GO:0032094; P:response to food; IDA:AgBase.
DR   GO; GO:1903576; P:response to L-arginine; IDA:AgBase.
DR   GO; GO:0009612; P:response to mechanical stimulus; IDA:AgBase.
DR   GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
DR   GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:AgBase.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR001400; Somatotropin/Prolactin.
DR   InterPro; IPR018116; Somatotropin_CS.
DR   PANTHER; PTHR11417; PTHR11417; 1.
DR   Pfam; PF00103; Hormone_1; 1.
DR   PRINTS; PR00836; SOMATOTROPIN.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00266; SOMATOTROPIN_1; 1.
DR   PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Hormone;
KW   Lactation; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:5507606"
FT   CHAIN           31..229
FT                   /note="Prolactin"
FT                   /id="PRO_0000032911"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8250856"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8250856"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8250856"
FT   DISULFID        34..41
FT                   /evidence="ECO:0000269|PubMed:4608931"
FT   DISULFID        88..204
FT                   /evidence="ECO:0000269|PubMed:4608931"
FT   DISULFID        221..229
FT                   /evidence="ECO:0000269|PubMed:4608931"
FT   CONFLICT        61
FT                   /note="D -> N (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   229 AA;  25793 MW;  E7E9BB6655A26F3D CRC64;
     MDSKGSSQKG SRLLLLLVVS NLLLCQGVVS TPVCPNGPGN CQVSLRDLFD RAVMVSHYIH
     DLSSEMFNEF DKRYAQGKGF ITMALNSCHT SSLPTPEDKE QAQQTHHEVL MSLILGLLRS
     WNDPLYHLVT EVRGMKGAPD AILSRAIEIE EENKRLLEGM EMIFGQVIPG AKETEPYPVW
     SGLPSLQTKD EDARYSAFYN LLHCLRRDSS KIDTYLKLLN CRIIYNNNC
 
 
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