GTHB2_CORAU
ID GTHB2_CORAU Reviewed; 142 AA.
AC P48251;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Gonadotropin subunit beta-2;
DE AltName: Full=GTH-II-beta;
DE AltName: Full=Gonadotropin beta-II chain;
DE Flags: Precursor;
GN Name=cgbb;
OS Coregonus autumnalis (Arctic cisco) (Salmo autumnalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Coregoninae; Coregonus.
OX NCBI_TaxID=27773;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=7990827;
RA Trofimova I.N., Belikov S.I.;
RT "Cloning and sequencing the cDNA for the beta-subunit of Baikal omul
RT gonadotropin.";
RL Mol. Biol. (Mosk.) 28:1052-1056(1994).
CC -!- FUNCTION: Involved in gametogenesis and steroidogenesis.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC {ECO:0000305}.
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DR EMBL; L23431; AAA68207.1; -; mRNA.
DR PIR; I50143; I50143.
DR AlphaFoldDB; P48251; -.
DR SMR; P48251; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR CDD; cd00069; GHB_like; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR006208; Glyco_hormone_CN.
DR InterPro; IPR001545; Gonadotropin_bsu.
DR InterPro; IPR018245; Gonadotropin_bsu_CS.
DR PANTHER; PTHR11515; PTHR11515; 1.
DR Pfam; PF00007; Cys_knot; 1.
DR SMART; SM00068; GHB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00261; GLYCO_HORMONE_BETA_1; 1.
DR PROSITE; PS00689; GLYCO_HORMONE_BETA_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hormone; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..142
FT /note="Gonadotropin subunit beta-2"
FT /id="PRO_0000011686"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..78
FT /evidence="ECO:0000250"
FT DISULFID 44..93
FT /evidence="ECO:0000250"
FT DISULFID 47..131
FT /evidence="ECO:0000250"
FT DISULFID 55..109
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 114..121
FT /evidence="ECO:0000250"
SQ SEQUENCE 142 AA; 15844 MW; 21105B70B410797D CRC64;
MLGLHVGTLM ISLFLCILLE PVEGSLMQPC QPINQTVSLE KEGCPTCLVI QTPICSGHCF
TKELVFKSPF STVYQHVCTY RDVRYETICL PDCSPWVDPH VTYPVALSCD CSLCNMDTSD
CTIESLQPDL CMTQRVLADG MW