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Database: UniProt
Entry: H3B686_LATCH
LinkDB: H3B686_LATCH
Original site: H3B686_LATCH 
ID   H3B686_LATCH            Unreviewed;       345 AA.
AC   H3B686;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Inhibin alpha chain {ECO:0000256|ARBA:ARBA00019280, ECO:0000256|PIRNR:PIRNR037328};
GN   Name=INHA {ECO:0000313|Ensembl:ENSLACP00000017407.2};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000017407.2, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000017407.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
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DR   EMBL; AFYH01036059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005991833.2; XM_005991771.2.
DR   AlphaFoldDB; H3B686; -.
DR   STRING; 7897.ENSLACP00000017407; -.
DR   Ensembl; ENSLACT00000017535.2; ENSLACP00000017407.2; ENSLACG00000015333.2.
DR   GeneID; 102356906; -.
DR   KEGG; lcm:102356906; -.
DR   CTD; 3623; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00390000005935; -.
DR   HOGENOM; CLU_064515_0_0_1; -.
DR   InParanoid; H3B686; -.
DR   OMA; PEHWTVF; -.
DR   OrthoDB; 5344254at2759; -.
DR   TreeFam; TF331531; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000015333; Expressed in pelvic fin.
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   CDD; cd13754; TGF_beta_INHA; 1.
DR   Gene3D; 2.60.120.970; -; 1.
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   InterPro; IPR017948; TGFb_CS.
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; PS00250; TGF_BETA_1; 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:UP000008672};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR037328};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..345
FT                   /note="Inhibin alpha chain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003580936"
FT   DOMAIN          229..345
FT                   /note="TGF-beta family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51362"
SQ   SEQUENCE   345 AA;  39037 MW;  3DEFBDE931494C6A CRC64;
     MQLKMVPFLV LMLCVQECVC TCSHHEVDKP VLIMILREHI LRSLGMEGSP SAQGETRNEM
     KGIHKRHVGD HQTHSHRGRP RVTEDTSQVI LFPTTDVPCE FTQLPQDKDD RDFTYLFQPS
     AHSLDRVVTN AHMWFYVGPS DSPSGQHHNL TTSPAELLIL SQQGHFTIAS TSMLLQDNWV
     IFRFAKPFLH YLSHKVFILQ VRCSTCPCIS DADKIPFIQS FTRLKNPDRS RRSSIPWSPE
     AVNLLQRPSE NGLLHSNCHK ASVNISFEEL GWGNWIIHPT FFTFNYCHGT CSSSDSLPYN
     LGIKLCCAAV PGTMNDLRVR TTSDGGYSFK YEAVPNIITN DCACM
//
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