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
//