ID   PRL_CAMDR               Reviewed;         199 AA.
AC   P22393;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Prolactin;
DE            Short=PRL;
GN   Name=PRL;
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9838;
RN   [1]
RP   PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-31.
RX   PubMed=2029533; DOI=10.1016/0167-4838(91)90549-f;
RA   Martinat N., Huet J.-C., Nespoulous C., Combarnous Y., Pernollet J.-C.;
RT   "Determination of the primary and secondary structures of the dromedary
RT   (Camelus dromedarius) prolactin and comparison with prolactins from other
RT   species.";
RL   Biochim. Biophys. Acta 1077:339-345(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-40.
RC   TISSUE=Pituitary;
RX   PubMed=2085952; DOI=10.1016/0305-0491(90)90105-3;
RA   Martinat N., Anouassi A., Huet J.-C., Pernollet J.-C., Combarnous Y.;
RT   "Purification and characterization of glycosylated and non-glycosylated
RT   forms of prolactin from the dromedary (Camelus dromedarius).";
RL   Comp. Biochem. Physiol. 97B:667-674(1990).
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   PIR; S15131; S15131.
DR   AlphaFoldDB; P22393; -.
DR   SMR; P22393; -.
DR   STRING; 9838.ENSCDRP00005026914; -.
DR   iPTMnet; P22393; -.
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; Glycoprotein; Hormone;
KW   Lactation; Phosphoprotein; Secreted.
FT   CHAIN           1..199
FT                   /note="Prolactin"
FT                   /id="PRO_0000181318"
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   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine; partial"
FT                   /evidence="ECO:0000269|PubMed:2029533"
FT   DISULFID        4..11
FT   DISULFID        58..174
FT   DISULFID        191..199
SQ   SEQUENCE   199 AA;  22971 MW;  EA382E98C4585B19 CRC64;
     LPICPSGAVN CQVSLRDLFD RAVILSHYIH NLSSEMFNEF DKRYAQGRGF MTKAINSCHT
     SSLSTPEDKE QAQQIHHEDL LNLVLRVLRS WNDPLYHLVT EVRGMQEAPD AILSRAIEIE
     EQNKRLLEGM EKIVGQVHPG VKENEIYSVW SGLPSLQMAD EDTRLFAFYN LLHCLRRDSH
     KIDNYLKLLK CRIIYDSNC