PRL_LOXAF
ID PRL_LOXAF Reviewed; 199 AA.
AC P10765;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Prolactin;
DE Short=PRL;
GN Name=PRL;
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Pituitary;
RX PubMed=2722400; DOI=10.1111/j.1399-3011.1989.tb00684.x;
RA Li C.H., Oosthuizen M.M.J., Chung D.;
RT "Primary structure of elephant pituitary prolactin.";
RL Int. J. Pept. Protein Res. 33:67-69(1989).
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 AlphaFoldDB; P10765; -.
DR SMR; P10765; -.
DR STRING; 9785.ENSLAFP00000016822; -.
DR eggNOG; ENOG502QYU3; Eukaryota.
DR InParanoid; P10765; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
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; Lactation;
KW Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..199
FT /note="Prolactin"
FT /id="PRO_0000181319"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01239"
FT DISULFID 4..11
FT /evidence="ECO:0000250"
FT DISULFID 58..174
FT /evidence="ECO:0000250"
FT DISULFID 191..199
FT /evidence="ECO:0000250"
SQ SEQUENCE 199 AA; 22673 MW; 6C43457310B9CCE7 CRC64;
IPVCPRGSVR CQVSLPDLFD RAVMLSHYIH SLSSDMFHEF NKQYALGRGF IPRAINSCHT
SSISTPEDKD QAQQTHHEVL MDLILGLLRS WNDPLDHLAS EVHSLPKAPS ALLTKATEVK
EENQRLLEGI EKIVDQVHPG AKENKAYSVW SGLPSLQTTD EDARLFAFYN LFRCLRRDSH
KIDSYLKLLK CRIVYNNNC