ID A0A3P9CAS1_9CICH Unreviewed; 347 AA.
AC A0A3P9CAS1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Inhibin alpha chain {ECO:0000256|ARBA:ARBA00019280, ECO:0000256|PIRNR:PIRNR037328};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005019212.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005019212.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005019212.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Inhibins and activins inhibit and activate, respectively, the
CC secretion of follitropin by the pituitary gland. Inhibins/activins are
CC involved in regulating a number of diverse functions such as
CC hypothalamic and pituitary hormone secretion, gonadal hormone
CC secretion, germ cell development and maturation, erythroid
CC differentiation, insulin secretion, nerve cell survival, embryonic
CC axial development or bone growth, depending on their subunit
CC composition. {ECO:0000256|PIRNR:PIRNR037328}.
CC -!- SUBUNIT: Dimeric, linked by one or more disulfide bonds. Inhibin A is a
CC dimer of alpha and beta-A. Inhibin B is a dimer of alpha and beta-B.
CC {ECO:0000256|ARBA:ARBA00011767}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the TGF-beta family.
CC {ECO:0000256|ARBA:ARBA00006656, ECO:0000256|RuleBase:RU000354}.
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 RefSeq; XP_004562606.1; XM_004562549.1.
DR RefSeq; XP_004562607.1; XM_004562550.1.
DR AlphaFoldDB; A0A3P9CAS1; -.
DR STRING; 106582.ENSMZEP00005019212; -.
DR Ensembl; ENSMZET00005019831.1; ENSMZEP00005019212.1; ENSMZEG00005014425.1.
DR GeneID; 101488051; -.
DR KEGG; mze:101488051; -.
DR CTD; 3623; -.
DR GeneTree; ENSGT00390000005935; -.
DR OrthoDB; 5344254at2759; -.
DR Proteomes; UP000265160; LG23.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:1900193; P:regulation of oocyte maturation; IEA:Ensembl.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR017175; Inhibin_asu.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR015615; TGF-beta-rel.
DR PANTHER; PTHR11848:SF117; INHIBIN ALPHA CHAIN; 1.
DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR PIRSF; PIRSF037328; Inhibin_alpha_subunit; 1.
DR PRINTS; PR00669; INHIBINA.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 3: Inferred from homology;
KW Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW ECO:0000256|PIRNR:PIRNR037328}; Hormone {ECO:0000256|PIRNR:PIRNR037328};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR037328};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..347
FT /note="Inhibin alpha chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018090659"
FT DOMAIN 228..347
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
SQ SEQUENCE 347 AA; 38285 MW; E59FD0D74AE9D080 CRC64;
MVSCTVLILG PLCIHGIIQA CMGEELSRGA VLSWFKVRVL EGLGLEEPPL STLQGPDADR
VPPDTRHLHQ RAHRTSRTSW VNPQTRPNQE SSQIILFPGS DCTKSDSAQG ETANRHMTYY
FQPSINSQDT VVTSAHFWFF AGEAVTANSS AQLFIVTTAL ERLQAAEAPS NSSSDGWTTY
HLDQNLLALV AEGPFLLQVH CPACQCHAGE PDKMPFLHLH VQPRGPSRSP RNAAVTIPWS
PSAIYLLQRP SQERPLHSDC HRAEIDISFE ELGWDNWIVH PKVLTFYYCH GNCSGGDLTT
AMLGITQCCA PVPGTMRSLR ITTTSDGGYS FKYETLPNII PEECTCI
//
