ID A0A1U7Q2B4_MESAU Unreviewed; 226 AA.
AC A0A1U7Q2B4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Prolactin {ECO:0000256|ARBA:ARBA00041065};
DE Flags: Precursor;
GN Name=LOC101843376 {ECO:0000313|RefSeq:NP_001268581.1};
GN Synonyms=PRL {ECO:0000313|RefSeq:NP_001268581.1}, prolactin
GN {ECO:0000313|RefSeq:NP_001268581.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:NP_001268581.1};
RN [1] {ECO:0000313|RefSeq:NP_001268581.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1954881;
RA Southard J.N., Sanchez-Jimenez F., Campbell G.T., Talamantes F.;
RT "Sequence and expression of hamster prolactin and growth hormone messenger
RT RNAs.";
RL Endocrinology 129:2965-2971(1991).
RN [2] {ECO:0000313|RefSeq:NP_001268581.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2017) to UniProtKB.
CC -!- FUNCTION: Prolactin acts primarily on the mammary gland by promoting
CC lactation. {ECO:0000256|ARBA:ARBA00037239}.
CC -!- SUBUNIT: Interacts with PRLR. {ECO:0000256|ARBA:ARBA00038619}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU003618}.
CC -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC {ECO:0000256|ARBA:ARBA00008474, ECO:0000256|RuleBase:RU003618}.
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DR RefSeq; NP_001268581.1; NM_001281652.1.
DR AlphaFoldDB; A0A1U7Q2B4; -.
DR SMR; A0A1U7Q2B4; -.
DR GeneID; 101843376; -.
DR KEGG; maua:101843376; -.
DR OrthoDB; 4765458at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
DR CDD; cd10288; prolactin_like; 1.
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:SF5; PROLACTIN; 1.
DR PANTHER; PTHR11417; SOMATOTROPIN,PROLACTIN; 1.
DR Pfam; PF00103; Hormone_1; 1.
DR PRINTS; PR00836; SOMATOTROPIN.
DR SUPFAM; SSF47266; 4-helical cytokines; 1.
DR PROSITE; PS00266; SOMATOTROPIN_1; 1.
DR PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hormone {ECO:0000256|RuleBase:RU003618};
KW Lactation {ECO:0000256|ARBA:ARBA00043262};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601400-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001268581.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR601400-1}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001268581.1"
FT CHAIN 30..226
FT /note="Prolactin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010542003"
FT CHAIN 30..226
FT /note="Prolactin"
FT /evidence="ECO:0000313|RefSeq:NP_001268581.1"
FT /id="PRO_5009993572"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR601400-1"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR601400-1"
SQ SEQUENCE 226 AA; 25582 MW; 2AD7B129612DCFCD CRC64;
MNSQGSDRKA VTLLLLVMSN LLFCQNAHPL PICPGGNCQM PLQELFDRVI MLSHYIYMLS
ADMFIELDKQ YAQDHEFIAK AISDCPTSSL ATPEGKEEAQ QVPPEVLLNL ILSLVHSWND
PLFQLVTEVD GIHEASDAII SRAKEIGEQN KRLLEGIEKI LGQAYPEAKG NEIYSVWSQF
PSLQGVDEES RDLAIYNKVR CLRRDSHKVD NYLKLLRCRV VHNNNC
//
