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Database: UniProt
Entry: A0A093IAW8_FULGA
LinkDB: A0A093IAW8_FULGA
Original site: A0A093IAW8_FULGA 
ID   A0A093IAW8_FULGA        Unreviewed;       424 AA.
AC   A0A093IAW8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Inhibin beta A chain {ECO:0000256|ARBA:ARBA00014111};
DE   AltName: Full=Activin beta-A chain {ECO:0000256|ARBA:ARBA00032434};
GN   ORFNames=N327_08291 {ECO:0000313|EMBL:KFV96603.1};
OS   Fulmarus glacialis (Northern fulmar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC   Fulmarus.
OX   NCBI_TaxID=30455 {ECO:0000313|EMBL:KFV96603.1, ECO:0000313|Proteomes:UP000053806};
RN   [1] {ECO:0000313|EMBL:KFV96603.1, ECO:0000313|Proteomes:UP000053806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N327 {ECO:0000313|EMBL:KFV96603.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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. Inhibins appear to oppose the functions of activins.
CC       {ECO:0000256|ARBA:ARBA00002588}.
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; KK585177; KFV96603.1; -; Genomic_DNA.
DR   RefSeq; XP_009586303.1; XM_009588008.1.
DR   AlphaFoldDB; A0A093IAW8; -.
DR   GeneID; 104084251; -.
DR   KEGG; fga:104084251; -.
DR   CTD; 3624; -.
DR   OrthoDB; 3015718at2759; -.
DR   Proteomes; UP000053806; Unassembled WGS sequence.
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   CDD; cd19404; TGF_beta_INHBA; 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; IPR000491; Inhibin_betaA.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR001111; TGF-b_propeptide.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848:SF133; INHIBIN BETA A CHAIN; 1.
DR   PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 1.
DR   PRINTS; PR00670; INHIBINBA.
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   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW   ECO:0000256|RuleBase:RU000354}; Hormone {ECO:0000256|ARBA:ARBA00022702};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053806};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..424
FT                   /note="Inhibin beta A chain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001887248"
FT   DOMAIN          304..424
FT                   /note="TGF-beta family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51362"
FT   REGION          176..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  47579 MW;  680216FB95F74CE2 CRC64;
     MPLLWKRGFL LVLCWIIVRS SPTPGSEGHS SVTDCPSCAL ATLSKDVPSS QPEMVEAVKK
     HILNMLHLRD RPNITQPVPK AALLNAIKKL HVGKVGEDGY VEIEDDVGRR AEMNEVVEQT
     SEIITFAESG TAKKMLHFEI SKEGSELSVV EHAEVWLFLK VSKANRSRTK VTIRLFQQQR
     QPKSNSEGAE DMEDGGLKGE RSETLISEKA VDTRKSTWHI FPVSSSVQRL LDQGKSSLDV
     RIACDLCQET GASLVLLGKK KKKEDDGEGK EKEAGEFTGE EEKEQSHRPF LMMLARHSED
     RQHRRRRRGL ECDGKVNICC KKQFFVSFKD IGWSDWIIAP TGYHANYCEG ECPSHIAGTS
     GSSLSFHSTV INHYRMRGHS PFANLKSCCV PTKLRPMSML YYDDGQNIIK KDIQNMIVEE
     CGCS
//
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