CRHBP_XENLA
ID CRHBP_XENLA Reviewed; 321 AA.
AC Q91653; A1L2Q7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Corticotropin-releasing factor-binding protein;
DE Short=CRF-BP;
DE Short=CRF-binding protein;
DE AltName: Full=Corticotropin-releasing hormone-binding protein;
DE Short=CRH-BP;
DE Flags: Precursor;
GN Name=crhbp; Synonyms=e;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8700860; DOI=10.1073/pnas.93.5.1924;
RA Brown D.D., Wang Z., Furlow J.D., Kanamori A., Schwartzman R.A., Remo B.F.,
RA Pinder A.;
RT "The thyroid hormone-induced tail resorption program during Xenopus laevis
RT metamorphosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1924-1929(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory bulb;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds CRF and inactivates it. May prevent inappropriate
CC pituitary-adrenal stimulation in pregnancy (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CRF-binding protein family. {ECO:0000305}.
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DR EMBL; U41858; AAC59874.1; -; mRNA.
DR EMBL; BC129661; AAI29662.1; -; mRNA.
DR RefSeq; NP_001079273.1; NM_001085804.1.
DR AlphaFoldDB; Q91653; -.
DR PRIDE; Q91653; -.
DR GeneID; 378555; -.
DR KEGG; xla:378555; -.
DR CTD; 378555; -.
DR Xenbase; XB-GENE-865598; crhbp.S.
DR OMA; AEPNQVI; -.
DR OrthoDB; 1361570at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 378555; Expressed in internal ear and 2 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051424; F:corticotropin-releasing hormone binding; IEA:InterPro.
DR InterPro; IPR008435; CRF-bd.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR10278; PTHR10278; 1.
DR Pfam; PF05428; CRF-BP; 1.
DR PIRSF; PIRSF009279; CRF_bd; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..321
FT /note="Corticotropin-releasing factor-binding protein"
FT /id="PRO_0000020998"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..80
FT /evidence="ECO:0000250"
FT DISULFID 103..140
FT /evidence="ECO:0000250"
FT DISULFID 182..204
FT /evidence="ECO:0000250"
FT DISULFID 237..264
FT /evidence="ECO:0000250"
FT DISULFID 277..317
FT /evidence="ECO:0000250"
SQ SEQUENCE 321 AA; 36295 MW; 7657861F32FDDE3E CRC64;
MTPASRPDWC LILLFLAVLR GESRYIQMRE AAEDALFLLN SDFKRELSEG QIYRRSLRCI
DMLSIEGQFT FQADRPQLHC ALFLIGEPEE FIIIEYNFVN IDCIGGDILK VFDGWIIKGE
KFPSSLDHPL STMERYTDIC EDGDVGSITR SSQNVAMIFF RVQQPGHGFT LTIRKIPNLF
PCNVISQSMN GRFTMITPHQ HRNCSFSIIY PVVIKIFDLT LGHFNELQLK KPPPKGCGDA
GDFVELLGGA GLDPSKMFPL ADLCHSFHGS AQMKIGCDNT VVRMVSSGNF INRVTFEYNQ
LDRQLEKKQG NSVEEACFPS D