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Database: UniProt
Entry: A0A384AK99_BALAS
LinkDB: A0A384AK99_BALAS
Original site: A0A384AK99_BALAS 
ID   A0A384AK99_BALAS        Unreviewed;       425 AA.
AC   A0A384AK99;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Inhibin beta A chain {ECO:0000256|ARBA:ARBA00014111};
DE   AltName: Full=Activin beta-A chain {ECO:0000256|ARBA:ARBA00032434};
GN   Name=INHBA {ECO:0000313|RefSeq:XP_007187796.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007187796.1};
RN   [1] {ECO:0000313|RefSeq:XP_007187796.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007187796.1};
RG   RefSeq;
RL   Submitted (JAN-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. 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   RefSeq; XP_007187796.1; XM_007187734.1.
DR   AlphaFoldDB; A0A384AK99; -.
DR   STRING; 310752.A0A384AK99; -.
DR   GeneID; 103010892; -.
DR   KEGG; bacu:103010892; -.
DR   CTD; 3624; -.
DR   InParanoid; A0A384AK99; -.
DR   OrthoDB; 3015718at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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:UP000261681};
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..425
FT                   /note="Inhibin beta A chain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016996471"
FT   DOMAIN          305..425
FT                   /note="TGF-beta family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51362"
FT   REGION          261..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  47636 MW;  6C3EDDE64DB1E18E CRC64;
     MPLLWLRGFL LVSCWIIVRS SPTPGSEGHS ATPDCPSCAL ATLPKDVPNS QPEMVEAVKK
     HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELMEQT
     SEIITFAESG TARKTLHFEI SKEGSDLSVV ERAEIWLFLK VPKANRTRTK VTIHLFQQQK
     HPQGSWDAGE EAEEVGLMGE RNEVLISEKA VDARKSTWHI FPVSSCIQRL LDQGKSSLDI
     RIACDQCHET GASLVLLGKK KKREEEGEGK KRDGEGGAGG DEEKEQSHRP FLMLQARQAE
     DHPHRRRRRG LECDGKVNIC CKKQFFVSFK DIGWNDWIIA PSGYHANYCE GECPSHIAGT
     SGSSLSFHST VINHYRMRGH SPFANLKSCC VPTKLRPMSM LYYDDGQNII KKDIQNMIVE
     ECGCS
//
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