CSH1_HUMAN
ID CSH1_HUMAN Reviewed; 217 AA.
AC P0DML2; P01243; Q0VDB1; Q14407;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Chorionic somatomammotropin hormone 1;
DE Short=Choriomammotropin;
DE AltName: Full=Lactogen;
DE AltName: Full=Placental lactogen;
DE Short=PL;
DE Flags: Precursor;
GN Name=CSH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CSH1).
RX PubMed=6208192; DOI=10.1016/s0021-9258(18)90667-8;
RA Selby M.J., Barta A., Baxter J.D., Bell G.I., Eberhardt N.L.;
RT "Analysis of a major human chorionic somatomammotropin gene. Evidence for
RT two functional promoter elements.";
RL J. Biol. Chem. 259:13131-13138(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=6300056; DOI=10.1016/s0021-9258(18)32734-0;
RA Barrera-Saldana H.A., Seeburg P.H., Saunders G.F.;
RT "Two structurally different genes produce the same secreted human placental
RT lactogen hormone.";
RL J. Biol. Chem. 258:3787-3793(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2744760; DOI=10.1016/0888-7543(89)90271-1;
RA Chen E.Y., Liao Y.C., Smith D.H., Barrera-Saldana H.A., Gelinas R.E.,
RA Seeburg P.H.;
RT "The human growth hormone locus: nucleotide sequence, biology, and
RT evolution.";
RL Genomics 4:479-497(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=7169009; DOI=10.1089/dna.1.1982.1.239;
RA Seeburg P.H.;
RT "The human growth hormone gene family: nucleotide sequences show recent
RT divergence and predict a new polypeptide hormone.";
RL DNA 1:239-249(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18473352; DOI=10.1002/humu.20767;
RA Sedman L., Padhukasahasram B., Kelgo P., Laan M.;
RT "Complex signatures of locus-specific selective pressures and gene
RT conversion on human growth hormone/chorionic somatomammotropin genes.";
RL Hum. Mutat. 29:1181-1193(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-217.
RX PubMed=593368; DOI=10.1038/270494a0;
RA Shine J., Seeburg P.H., Martial J.A., Baxter J.D., Goodman H.M.;
RT "Construction and analysis of recombinant DNA for human chorionic
RT somatomammotropin.";
RL Nature 270:494-499(1977).
RN [9]
RP PROTEIN SEQUENCE OF 27-217.
RX PubMed=4712450; DOI=10.1016/s0003-9861(73)80012-8;
RA Li C.H., Dixon J.S., Chung D.;
RT "Amino acid sequence of human chorionic somatomammotropin.";
RL Arch. Biochem. Biophys. 155:95-110(1973).
RN [10]
RP PROTEIN SEQUENCE OF 27-217.
RX PubMed=5286363; DOI=10.1038/newbio233059a0;
RA Sherwood L.M., Handwerger S., McLaurin W.D., Lanner M.;
RT "Amino-acid sequence of human placental lactogen.";
RL Nature New Biol. 233:59-61(1971).
RN [11]
RP ERRATUM OF PUBMED:5286363.
RA Sherwood L.M., Handwerger S., McLaurin W.D., Lanner M.;
RL Nature New Biol. 235:64-64(1972).
RN [12]
RP INTERCHAIN DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=438159; DOI=10.1016/s0021-9258(18)50655-4;
RA Schneider A.B., Kowalski K., Russell J., Sherwood L.M.;
RT "Identification of the interchain disulfide bonds of dimeric human
RT placental lactogen.";
RL J. Biol. Chem. 254:3782-3787(1979).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 27-217, FUNCTION, ZINC-BINDING
RP SITES, AND DISULFIDE BONDS.
RX PubMed=16546209; DOI=10.1016/j.jmb.2006.02.038;
RA Walsh S.T., Kossiakoff A.A.;
RT "Crystal structure and site 1 binding energetics of human placental
RT lactogen.";
RL J. Mol. Biol. 358:773-784(2006).
CC -!- FUNCTION: Produced only during pregnancy and is involved in stimulating
CC lactation, fetal growth and metabolism. Does not interact with GHR but
CC only activates PRLR through zinc-induced dimerization.
CC {ECO:0000269|PubMed:16546209}.
CC -!- SUBUNIT: Can be found in a monomeric as well as dimeric form.
CC {ECO:0000269|PubMed:438159}.
CC -!- INTERACTION:
CC P0DML2; O00233: PSMD9; NbExp=5; IntAct=EBI-13375302, EBI-750973;
CC P0DML2; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-13375302, EBI-744081;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: CSH1 sequence only differs from CSH2 sequence in 1 aa.
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; K02401; AAA52115.1; -; Genomic_DNA.
DR EMBL; J03071; AAA52551.1; -; Genomic_DNA.
DR EMBL; J00118; AAA98621.1; -; mRNA.
DR EMBL; BT006926; AAP35572.1; -; mRNA.
DR EMBL; BC002717; AAH02717.1; -; mRNA.
DR EMBL; BC005921; AAH05921.1; -; mRNA.
DR EMBL; BC020756; AAH20756.1; -; mRNA.
DR EMBL; BC062775; AAH62775.1; -; mRNA.
DR CCDS; CCDS11649.1; -.
DR RefSeq; NP_001308.1; NM_001317.5.
DR PDB; 1Z7C; X-ray; 2.00 A; A=27-217.
DR PDBsum; 1Z7C; -.
DR AlphaFoldDB; P0DML2; -.
DR SMR; P0DML2; -.
DR BioGRID; 107829; 14.
DR IntAct; P0DML2; 5.
DR STRING; 9606.ENSP00000316416; -.
DR iPTMnet; P0DML2; -.
DR MetOSite; P0DML2; -.
DR PhosphoSitePlus; P0DML2; -.
DR BioMuta; CSH1; -.
DR MassIVE; P0DML2; -.
DR PaxDb; P0DML2; -.
DR PeptideAtlas; P0DML2; -.
DR PRIDE; P0DML2; -.
DR ABCD; P0DML2; 1 sequenced antibody.
DR Antibodypedia; 18837; 452 antibodies from 32 providers.
DR DNASU; 1442; -.
DR Ensembl; ENST00000316193.13; ENSP00000316416.8; ENSG00000136488.15.
DR GeneID; 1442; -.
DR KEGG; hsa:1442; -.
DR MANE-Select; ENST00000316193.13; ENSP00000316416.8; NM_001317.6; NP_001308.1.
DR UCSC; uc002jcs.3; human.
DR CTD; 1442; -.
DR DisGeNET; 1442; -.
DR GeneCards; CSH1; -.
DR HGNC; HGNC:2440; CSH1.
DR HPA; ENSG00000136488; Tissue enriched (placenta).
DR MIM; 150200; gene.
DR neXtProt; NX_P0DML2; -.
DR OpenTargets; ENSG00000136488; -.
DR VEuPathDB; HostDB:ENSG00000136488; -.
DR eggNOG; ENOG502R5GJ; Eukaryota.
DR GeneTree; ENSGT00950000182818; -.
DR HOGENOM; CLU_088274_2_1_1; -.
DR OMA; WIRCILR; -.
DR OrthoDB; 1190548at2759; -.
DR PhylomeDB; P0DML2; -.
DR PathwayCommons; P0DML2; -.
DR Reactome; R-HSA-1170546; Prolactin receptor signaling.
DR Reactome; R-HSA-982772; Growth hormone receptor signaling.
DR SignaLink; P0DML2; -.
DR BioGRID-ORCS; 1442; 13 hits in 969 CRISPR screens.
DR ChiTaRS; CSH1; human.
DR GenomeRNAi; 1442; -.
DR Pharos; P0DML2; Tbio.
DR PRO; PR:P0DML2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P0DML2; protein.
DR Bgee; ENSG00000136488; Expressed in placenta and 35 other tissues.
DR ExpressionAtlas; P0DML2; baseline and differential.
DR Genevisible; P0DML2; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0031904; C:endosome lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IDA:AgBase.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0005131; F:growth hormone receptor binding; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045927; P:positive regulation of growth; IBA:GO_Central.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IBA:GO_Central.
DR GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
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 3D-structure; Direct protein sequencing; Disulfide bond; Hormone;
KW Metal-binding; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:4712450,
FT ECO:0000269|PubMed:5286363"
FT CHAIN 27..217
FT /note="Chorionic somatomammotropin hormone 1"
FT /id="PRO_0000032958"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT DISULFID 79..191
FT /evidence="ECO:0000269|PubMed:16546209"
FT DISULFID 208..215
FT /note="In monomeric form"
FT /evidence="ECO:0000269|PubMed:16546209"
FT DISULFID 208
FT /note="Interchain (with C-215); in dimeric form"
FT /evidence="ECO:0000269|PubMed:16546209"
FT DISULFID 215
FT /note="Interchain (with C-208); in dimeric form"
FT /evidence="ECO:0000269|PubMed:16546209"
FT CONFLICT 84
FT /note="I -> T (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="Missing (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="Missing (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..136
FT /note="SDD -> BBS (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 32..61
FT /evidence="ECO:0007829|PDB:1Z7C"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1Z7C"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1Z7C"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1Z7C"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:1Z7C"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:1Z7C"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:1Z7C"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1Z7C"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1Z7C"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1Z7C"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:1Z7C"
FT HELIX 181..210
FT /evidence="ECO:0007829|PDB:1Z7C"
SQ SEQUENCE 217 AA; 25020 MW; 235B0DC7A713F431 CRC64;
MAPGSRTSLL LAFALLCLPW LQEAGAVQTV PLSRLFDHAM LQAHRAHQLA IDTYQEFEET
YIPKDQKYSF LHDSQTSFCF SDSIPTPSNM EETQQKSNLE LLRISLLLIE SWLEPVRFLR
SMFANNLVYD TSDSDDYHLL KDLEEGIQTL MGRLEDGSRR TGQILKQTYS KFDTNSHNHD
ALLKNYGLLY CFRKDMDKVE TFLRMVQCRS VEGSCGF
