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GTHB2_CLAGA
ID   GTHB2_CLAGA             Reviewed;         138 AA.
AC   P53543;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
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   Clarias gariepinus (North African catfish) (Silurus gariepinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Clariidae; Clarias.
OX   NCBI_TaxID=13013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Rebers F.E.M., Tensen C.P., Schulz R.W., Goos H.J.T., Bogerd J.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 22-138.
RC   TISSUE=Pituitary;
RX   PubMed=1426937; DOI=10.1016/0016-6480(92)90039-m;
RA   Koide Y., Noso T., Schouten G., Peute J., Zandbergen M.A., Bogerd J.,
RA   Schulz R.W., Kawauchi H., Goos H.J.;
RT   "Maturational gonadotropin from the African catfish, Clarias gariepinus:
RT   purification, characterization, localization, and biological activity.";
RL   Gen. Comp. Endocrinol. 87:327-341(1992).
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; X97761; CAA66359.1; -; mRNA.
DR   AlphaFoldDB; P53543; -.
DR   SMR; P53543; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031762; F:follicle-stimulating hormone receptor binding; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0031775; F:lutropin-choriogonadotropic hormone receptor binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:2000836; P:positive regulation of androgen secretion; ISS:UniProtKB.
DR   GO; GO:2000866; P:positive regulation of estradiol secretion; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:1426937"
FT   CHAIN           22..138
FT                   /note="Gonadotropin subunit beta-2"
FT                   /id="PRO_0000011683"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..106
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        111..118
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15772 MW;  670D81FAFAC6880E CRC64;
     MPASSYFLLF FFMNFFSPAQ SYLLTHCEPV NETVSVEKDG CPKCLAFQTS ICSGHCFTKE
     PVYKSPFSSI YQHVCTYRDV RYETIRLPDC RPGVDPHVTY PVALSCECSL CTMDTSDCTI
     ESLNPDFCMT QKEFILDY
 
 
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