ID   PRL2_ONCKE              Reviewed;         210 AA.
AC   P09584;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Prolactin-2;
DE   AltName: Full=Prolactin II;
DE            Short=PRL-II;
DE   Flags: Precursor;
GN   Name=prl2;
OS   Oncorhynchus keta (Chum salmon) (Salmo keta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Kuwana Y., Kuga T., Sekine S., Sato M., Kawauchi H., Itoh S.;
RT   "Cloning and expression of cDNA for salmon prolactin in Escherichia coli.";
RL   Agric. Biol. Chem. 52:1033-1039(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-210, AND DISULFIDE BONDS.
RC   TISSUE=Pituitary;
RX   PubMed=3947078; DOI=10.1016/0003-9861(86)90621-1;
RA   Yasuda A., Itoh H., Kawauchi H.;
RT   "Primary structure of chum salmon prolactins: occurrence of highly
RT   conserved regions.";
RL   Arch. Biochem. Biophys. 244:528-541(1986).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
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DR   EMBL; D00249; BAA00180.1; -; mRNA.
DR   PIR; I51084; I51084.
DR   AlphaFoldDB; P09584; -.
DR   SMR; P09584; -.
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; IMP: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; IMP: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; IMP: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; 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   Direct protein sequencing; Disulfide bond; Hormone; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:3947078"
FT   CHAIN           24..210
FT                   /note="Prolactin-2"
FT                   /id="PRO_0000032940"
FT   DISULFID        69..183
FT                   /evidence="ECO:0000269|PubMed:3947078"
FT   DISULFID        200..210
FT                   /evidence="ECO:0000269|PubMed:3947078"
FT   CONFLICT        85..86
FT                   /note="RV -> KR (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   210 AA;  23431 MW;  6CC0DBB0CF75CA14 CRC64;
     MARRSQGTKL HLAVLCLVVS CHAIGLSDLM ERASQRSDKL HSLSTSLNKD LDSHFPPMGR
     VMMPRPSMCH TSSLQIPKDK EQALRVSENE LISLARSLLL AWNDPLLLLS SEAPTLPHPS
     NGDISSKIRE LQDYSKSLGD GLDILVNKMG PSSQYISSIP FKGGDLGNDK TSRLINFHFL
     MSCFRRDSHK IDSFLKVLRC RATKMRPETC