ID X2FW28_9TELE Unreviewed; 392 AA.
AC X2FW28;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Inhibin beta B chain {ECO:0000256|ARBA:ARBA00014337};
DE AltName: Full=Activin beta-B chain {ECO:0000256|ARBA:ARBA00032422};
OS Carassius auratus x Cyprinus carpio x Carassius cuvieri (triploid hybrids
OS of tetraploid and Japanese crucian carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinoidei intergeneric hybrids.
OX NCBI_TaxID=211491 {ECO:0000313|EMBL:AHN09805.1};
RN [1] {ECO:0000313|EMBL:AHN09805.1}
RP NUCLEOTIDE SEQUENCE.
RA Tao M., Liu S., Song C., Zhang Z., Chen J.;
RT "Differential expression of activin beta A and beta B in sterile triploids
RT and fertile tetraploids.";
RL Submitted (JAN-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ093507; AHN09805.1; -; mRNA.
DR AlphaFoldDB; X2FW28; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR CDD; cd19405; TGF_beta_INHBB; 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; IPR000381; INHBB_C.
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:SF29; INHIBIN BETA B CHAIN; 1.
DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR PRINTS; PR00671; INHIBINBB.
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}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..392
FT /note="Inhibin beta B chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004949822"
FT DOMAIN 273..392
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
SQ SEQUENCE 392 AA; 43841 MW; 3CC453BA24D2B583 CRC64;
MDTVFKKMSI PILSVTCLMA CILSVQCSLG AETLSQESQC ASCGLGHPDD SGRMDTDFLE
AVKRHILNRL QMRERPNITH PIPKAAMVTA LRKLHAGKVR EDGRVEIPNF DGHAAHNEVQ
EETSEIISFA ESDDVTPSKS SLYFLISNEG NQNLYVLQAN LWLYFKLLPG TQEKGLRRKV
TVRVRSYEPG GQNVHWPMME KRVELKRSGW HTFPVSEAVR EMLAKGGRRQ DLDIHCEGCE
AANVLPILVD PSDPSHRPFL VVRAQQADGK HRIRKRGLEC DGTNGGLCCR QQFYIDFRLI
GWNDWIIAPA GYYGNYCEGS CPAYMAGVPG SASSFHTAVV NQYRMRGMSP GSVNSCCIPT
KLSTMSMLYF DDEYNIVKRD VPNMIVEECG CA
//
