ID Q2LAG2_CTEID Unreviewed; 404 AA.
AC Q2LAG2;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Inhibin beta A chain {ECO:0000256|ARBA:ARBA00014111};
DE AltName: Full=Activin beta-A chain {ECO:0000256|ARBA:ARBA00032434};
OS Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Ctenopharyngodon.
OX NCBI_TaxID=7959 {ECO:0000313|EMBL:ABC72405.1};
RN [1] {ECO:0000313|EMBL:ABC72405.1}
RP NUCLEOTIDE SEQUENCE.
RA Fung S.K., Wong A.O.L.;
RT "Molecular cloning and functional characterization of grass carp activin
RT beta a precursor.";
RL Submitted (DEC-2005) 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; DQ340763; ABC72405.1; -; mRNA.
DR AlphaFoldDB; Q2LAG2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..404
FT /note="Inhibin beta A chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004212125"
FT DOMAIN 282..404
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT REGION 22..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 44300 MW; DBCD9624A7E1B726 CRC64;
MSSLTLVTGV LLLSGCLSGG CSPTPAESGS QGAGHPDDPA VTPCPSCALA QRQKDSEEQT
DMVEAVKRHI LNMLHLNTRP NVTHPVPRAA LLNAIRKLHV GRVGEDGTVE IEEDGGGLGE
REQPEEQPFE IITFAEPGDA PDVMKFDISK EGNTLSVVEQ ANVWLFLKVA KGNRGKGKVS
IQLLQHGKAD PVSTDGSQEL VVSEKTVDTR RSGWHTLPVP RMVQTLLDGD SSFLSLRVSC
PLCAEAGAVP ILVPAEGNKG KEREQSHRPF LMVVLKPAEE HQHRRSKRGL ECDGKIRVCC
KRQFYVNFKD IGWSDWIIAP SGYHANYCEG DCPSHVASIT GSALSFHSTV INHYRMRGYS
PFTNIKSCCV PTRLRAMSML YYNEEQKIIK KDIQNMIVEE CGCS
//
