ID   PRL_CORAU               Reviewed;         210 AA.
AC   P34181;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Prolactin;
DE            Short=PRL;
DE   Flags: Precursor;
GN   Name=prl;
OS   Coregonus autumnalis (Arctic cisco) (Salmo autumnalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Coregoninae; Coregonus.
OX   NCBI_TaxID=27773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=8364687;
RA   Trofimova I.N., Kuznedelov K.D., Kumarev V.P., Golovin S.Y.;
RT   "Molecular cloning and sequencing of omul prolactin cDNA.";
RL   Mol. Mar. Biol. Biotechnol. 2:41-43(1993).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Pituitary gland.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z23114; CAA80660.1; -; mRNA.
DR   EMBL; L23433; AAA51434.1; -; mRNA.
DR   PIR; S34351; S34351.
DR   AlphaFoldDB; P34181; -.
DR   SMR; P34181; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0005148; F:prolactin receptor binding; ISS:AgBase.
DR   GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; ISS:AgBase.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISS:AgBase.
DR   GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; ISS:AgBase.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR   GO; GO:0070665; P:positive regulation of leukocyte proliferation; ISS:AgBase.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:AgBase.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISS:AgBase.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISS:AgBase.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; ISS:AgBase.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:AgBase.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:AgBase.
DR   GO; GO:0002637; P:regulation of immunoglobulin production; ISS: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   2: Evidence at transcript level;
KW   Disulfide bond; Hormone; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..210
FT                   /note="Prolactin"
FT                   /id="PRO_0000032933"
FT   DISULFID        69..183
FT                   /evidence="ECO:0000250"
FT   DISULFID        200..210
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  23406 MW;  6BD521E179D18A2D CRC64;
     MARRSQGTKL HLAVLCLVVS CHAIGLSDLM ERASQRSDKL HSLSTSLTKD LDSHFPPMGR
     VMMPRPSMCH TSSLQTPKDK EQALRVSENE LISLARSLLL AWNDPLLLLS SEAPTLPHPS
     NGDISSKIRE LQDYSKSLGD GLDILVNKMG PSSQYISSIP FKGGDLGNDK TSRLINFHFL
     MSCFRRDSHK IDSFLKVLRC RATKMRPETC