ID A0A091CRZ9_FUKDA Unreviewed; 424 AA.
AC A0A091CRZ9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Inhibin beta A chain {ECO:0000256|ARBA:ARBA00014111};
DE AltName: Full=Activin beta-A chain {ECO:0000256|ARBA:ARBA00032434};
GN ORFNames=H920_17999 {ECO:0000313|EMBL:KFO20613.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO20613.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO20613.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO20613.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN124686; KFO20613.1; -; Genomic_DNA.
DR RefSeq; XP_010609160.1; XM_010610858.1.
DR AlphaFoldDB; A0A091CRZ9; -.
DR STRING; 885580.ENSFDAP00000022924; -.
DR Ensembl; ENSFDAT00000009294; ENSFDAP00000022924; ENSFDAG00000021196.
DR GeneID; 104853030; -.
DR CTD; 3624; -.
DR eggNOG; KOG3900; Eukaryota.
DR OMA; MAKYFIT; -.
DR OrthoDB; 3015718at2759; -.
DR Proteomes; UP000028990; 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 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:UP000028990};
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_5001872618"
FT DOMAIN 304..424
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT REGION 259..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 47294 MW; 8A13A6146652A384 CRC64;
MPLLWLRGFL WASCWIIVRS SPTPGSEGHS AAPNCPSCAL ATLPKDVPNS QPEMVEAVKK
HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELLEQT
SEIITFAESG AARKTLHFEI SKEGSDLSVV ERAEVWLFLK VPKANRTRTK VTIRLFQQQK
HPQGSLDAGD EAEEVGLKGE RSELLLSEKA VDARKSTWHI FPVSSSIQRL LDQGKTSLDV
RIACEQCQDS GASLVLLGKK KKKEEEGDGK KQGGGAGAVE EEKEQSHRPF LMLQARQSED
HPHRRRRRGL ECDGKVNICC KKQFFVSFKD IGWNDWIIAP SGYHANYCEG ECPSHIAGTS
GSSLSFHSTV INHYRMRGHS PFANLKSCCV PTKLRPMSML YYDDGQNIIK KDIQNMIVEE
CGCS
//
