P01243 (CSH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chorionic somatomammotropin hormone
Short name=Choriomammotropin

Alternative name(s):
Lactogen
Placental lactogen
Short name=PL

Gene names

Name:	CSH1
AND
Name:	CSH2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Produced only during pregnancy and is involved in stimulating lactation, fetal growth and metabolism. Does not interact with GHR but only activates PRLR through zinc-induced dimerization. Ref.14
Subcellular location	Secreted.
Miscellaneous	The sequence of CSH1 is shown.
Sequence similarities	Belongs to the somatotropin/prolactin family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hormone
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade involved in growth hormone signaling pathway Traceable author statement. Source: Reactome female pregnancy Traceable author statement PubMed 1378436. Source: ProtInc
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.10 Ref.11

Chain

27 – 217

191

Chorionic somatomammotropin hormone Ref.13

PRO_0000032958

Sites

Metal binding

44

1

Zinc

Metal binding

200

1

Zinc

Amino acid modifications

Disulfide bond

79 ↔ 191

Ref.13 Ref.14

Disulfide bond

208 ↔ 215

In monomeric form Ref.13 Ref.14

Disulfide bond

208

Interchain (with C-215); in dimeric form Ref.13 Ref.14

Disulfide bond

215

Interchain (with C-208); in dimeric form Ref.13 Ref.14

Natural variations

Natural variant

3

1

P → A in CSH2. Ref.8
Corresponds to variant rs1130686 [ dbSNP | Ensembl ].

VAR_007166

Natural variant

104 – 105

2

IS → L in CSH2.

VAR_007167

Experimental info

Sequence conflict

84

1

I → T AA sequence Ref.11

Sequence conflict

95

1

Missing AA sequence Ref.11

Sequence conflict

116

1

Missing AA sequence Ref.11

Sequence conflict

134 – 136

3

SDD → BBS AA sequence Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

217

Helix Strand Turn

Details...

Helix

32 – 61

30

Helix

64 – 66

3

Turn

67 – 70

4

Helix

80 – 82

3

Helix

99 – 110

12

Turn

111 – 114

4

Helix

115 – 123

9

Beta strand

124 – 126

3

Turn

133 – 135

3

Helix

136 – 138

3

Helix

139 – 154

16

Helix

181 – 210

30

Sequences

	Sequence		Length	Mass (Da)
	P01243 [UniParc]. Last modified April 1, 1988. Version 2. Checksum: 235B0DC7A713F431	FASTA	217	25,020
	10 20 30 40 50 60 MAPGSRTSLL LAFALLCLPW LQEAGAVQTV PLSRLFDHAM LQAHRAHQLA IDTYQEFEET 70 80 90 100 110 120 YIPKDQKYSF LHDSQTSFCF SDSIPTPSNM EETQQKSNLE LLRISLLLIE SWLEPVRFLR 130 140 150 160 170 180 SMFANNLVYD TSDSDDYHLL KDLEEGIQTL MGRLEDGSRR TGQILKQTYS KFDTNSHNHD 190 200 210 ALLKNYGLLY CFRKDMDKVE TFLRMVQCRS VEGSCGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of a major human chorionic somatomammotropin gene. Evidence for two functional promoter elements." Selby M.J., Barta A., Baxter J.D., Bell G.I., Eberhardt N.L. J. Biol. Chem. 259:13131-13138(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CSH1).
[2]	"The human growth hormone gene locus: structure, evolution, and allelic variations." Hirt H., Kimelman J., Birnbaum M.J., Chen E.Y., Seeburg P.H., Eberhardt N.L., Barta A. DNA 6:59-70(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CSH2).
[3]	"Two structurally different genes produce the same secreted human placental lactogen hormone." Barrera-Saldana H.A., Seeburg P.H., Saunders G.F. J. Biol. Chem. 258:3787-3793(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]	"The human growth hormone locus: nucleotide sequence, biology, and evolution." Chen E.Y., Liao Y.C., Smith D.H., Barrera-Saldana H.A., Gelinas R.E., Seeburg P.H. Genomics 4:479-497(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CSH1 AND CSH2).
[5]	"The human growth hormone gene family: nucleotide sequences show recent divergence and predict a new polypeptide hormone." Seeburg P.H. DNA 1:239-249(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[6]	"Complex signatures of locus-specific selective pressures and gene conversion on human growth hormone/chorionic somatomammotropin genes." Sedman L., Padhukasahasram B., Kelgo P., Laan M. Hum. Mutat. 29:1181-1193(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-3. Tissue: Placenta and Uterus.
[9]	"Construction and analysis of recombinant DNA for human chorionic somatomammotropin." Shine J., Seeburg P.H., Martial J.A., Baxter J.D., Goodman H.M. Nature 270:494-499(1977) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-217.
[10]	"Amino acid sequence of human chorionic somatomammotropin." Li C.H., Dixon J.S., Chung D. Arch. Biochem. Biophys. 155:95-110(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-217.
[11]	"Amino-acid sequence of human placental lactogen." Sherwood L.M., Handwerger S., McLaurin W.D., Lanner M. Nature New Biol. 233:59-61(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-217.
[12]	Erratum Sherwood L.M., Handwerger S., McLaurin W.D., Lanner M. Nature New Biol. 235:64-64(1972)
[13]	"Identification of the interchain disulfide bonds of dimeric human placental lactogen." Schneider A.B., Kowalski K., Russell J., Sherwood L.M. J. Biol. Chem. 254:3782-3787(1979) [PubMed] [Europe PMC] [Abstract] Cited for: INTERCHAIN DISULFIDE BONDS.
[14]	"Crystal structure and site 1 binding energetics of human placental lactogen." Walsh S.T., Kossiakoff A.A. J. Mol. Biol. 358:773-784(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 27-217, FUNCTION, ZINC-BINDING SITES, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00573 mRNA. Translation: CAA23836.1.
J00289 Genomic DNA. Translation: AAA98747.1.
K02401 Genomic DNA. Translation: AAA52115.1.
M15894 Genomic DNA. Translation: AAA52116.1.
J03071 Genomic DNA. Translation: AAA52551.1.
J03071 Genomic DNA. Translation: AAA52553.1.
J00118 mRNA. Translation: AAA98621.1.
EU421716 Genomic DNA. Translation: ABZ88723.1.
BT006926 mRNA. Translation: AAP35572.1.
BC002717 mRNA. Translation: AAH02717.1.
BC005921 mRNA. Translation: AAH05921.1.
BC020756 mRNA. Translation: AAH20756.1.
BC022044 mRNA. Translation: AAH22044.1.
BC035965 mRNA. Translation: AAH35965.1.
BC062775 mRNA. Translation: AAH62775.1.
BC119748 mRNA. Translation: AAI19749.1.

IPI

IPI00000891.

PIR

A26449.
LCHUC. C32435.
E32435.

RefSeq

NP_001308.1. NM_001317.5.
NP_066271.1. NM_020991.3.

UniGene

Hs.654390.
Hs.654515.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z7C	X-ray	2.00	A	27-217	[»]

ProteinModelPortal

P01243.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1190951.

STRING

9606.ENSP00000333268.

Polymorphism databases

DMDM

130299.

Proteomic databases

PRIDE

P01243.

Protocols and materials databases

DNASU

1442.
1443.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316193; ENSP00000316416; ENSG00000136488.
ENST00000392886; ENSP00000376623; ENSG00000213218.

GeneID

1442.
1443.

KEGG

hsa:1442.
hsa:1443.

UCSC

uc002jch.3. human.

Organism-specific databases

CTD

1442.
1443.

GeneCards

GC17M061949.
GC17M061972.

HGNC

HGNC:2440. CSH1.
HGNC:2441. CSH2.

HPA

CAB026374.
HPA043715.

MIM

118820. gene.
150200. gene.

neXtProt

NX_P01243.

PharmGKB

PA26944.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HOG000068443.

HOVERGEN

HBG011318.

KO

K05438.

OMA

AAFCYSE.

OrthoDB

EOG42FSJN.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P01243.

Bgee

P01243.

CleanEx

HS_CSH1.
HS_CSH2.

Genevestigator

P01243.

GermOnline

ENSG00000136488. Homo sapiens.

Family and domain databases

Gene3D

1.20.1250.10. 1 hit.

InterPro

IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001400. Somatotropin.
IPR018116. Somatotropin_CS.
[Graphical view]

PANTHER

PTHR11417. PTHR11417. 1 hit.

Pfam

PF00103. Hormone_1. 1 hit.
[Graphical view]

PRINTS

PR00836. SOMATOTROPIN.

SUPFAM

SSF47266. 4_helix_cytokine. 1 hit.

PROSITE

PS00266. SOMATOTROPIN_1. 1 hit.
PS00338. SOMATOTROPIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CSH1. human.
CSH2. human.

EvolutionaryTrace

P01243.

NextBio

5911.

SOURCE

Search...

Entry information

Entry name

CSH_HUMAN

Accession

Primary (citable) accession number: P01243
Secondary accession number(s): Q0VDB1, Q14407

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	May 1, 2013
This is version 150 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.