ID   CRHBP_HUMAN             Reviewed;         322 AA.
AC   P24387; Q53F32; Q6FHT5;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   24-JAN-2024, entry version 174.
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=CRFBP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=1846945; DOI=10.1038/349423a0;
RA   Potter E., Behan D.P., Fischer W.H., Linton E.A., Lowry P.J., Vale W.W.;
RT   "Cloning and characterization of the cDNAs for human and rat corticotropin
RT   releasing factor-binding proteins.";
RL   Nature 349:423-426(1991).
RN   [2]
RP   SEQUENCE REVISION TO 47-48 AND 248, AND DISULFIDE BONDS.
RX   PubMed=8307998; DOI=10.1016/s0021-9258(17)41780-7;
RA   Fischer W.H., Behan D.P., Park M., Potter E., Lowry P.J., Vale W.W.;
RT   "Assignment of disulfide bonds in corticotropin-releasing factor-binding
RT   protein.";
RL   J. Biol. Chem. 269:4313-4316(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hippocampus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX   PubMed=8198617; DOI=10.1006/geno.1993.1141;
RA   Behan D.P., Potter E., Lewis K.A., Jenkins N.A., Copeland N.G., Lowry P.J.,
RA   Vale W.W.;
RT   "Cloning and structure of the human corticotrophin releasing factor-binding
RT   protein gene (CRHBP).";
RL   Genomics 16:63-68(1993).
CC   -!- FUNCTION: Binds CRF and inactivates it. May prevent inappropriate
CC       pituitary-adrenal stimulation in pregnancy.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the CRF-binding protein family. {ECO:0000305}.
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DR   EMBL; X58022; CAA41086.1; ALT_SEQ; mRNA.
DR   EMBL; S60697; AAD13916.1; -; Genomic_DNA.
DR   EMBL; CR541666; CAG46467.1; -; mRNA.
DR   EMBL; AK223457; BAD97177.1; -; mRNA.
DR   EMBL; CH471084; EAW95786.1; -; Genomic_DNA.
DR   EMBL; BC018038; AAH18038.1; -; mRNA.
DR   CCDS; CCDS4034.1; -.
DR   PIR; S13640; S13640.
DR   RefSeq; NP_001873.2; NM_001882.3.
DR   AlphaFoldDB; P24387; -.
DR   BioGRID; 107783; 15.
DR   IntAct; P24387; 11.
DR   STRING; 9606.ENSP00000274368; -.
DR   BindingDB; P24387; -.
DR   ChEMBL; CHEMBL5930; -.
DR   GlyConnect; 1932; 6 N-Linked glycans (1 site).
DR   GlyCosmos; P24387; 1 site, 6 glycans.
DR   GlyGen; P24387; 1 site, 6 N-linked glycans (1 site).
DR   iPTMnet; P24387; -.
DR   PhosphoSitePlus; P24387; -.
DR   BioMuta; CRHBP; -.
DR   DMDM; 544099; -.
DR   MassIVE; P24387; -.
DR   PaxDb; 9606-ENSP00000274368; -.
DR   PeptideAtlas; P24387; -.
DR   ProteomicsDB; 54201; -.
DR   Antibodypedia; 24474; 228 antibodies from 26 providers.
DR   DNASU; 1393; -.
DR   Ensembl; ENST00000274368.9; ENSP00000274368.4; ENSG00000145708.11.
DR   GeneID; 1393; -.
DR   KEGG; hsa:1393; -.
DR   MANE-Select; ENST00000274368.9; ENSP00000274368.4; NM_001882.4; NP_001873.2.
DR   UCSC; uc003ker.4; human.
DR   AGR; HGNC:2356; -.
DR   CTD; 1393; -.
DR   DisGeNET; 1393; -.
DR   GeneCards; CRHBP; -.
DR   HGNC; HGNC:2356; CRHBP.
DR   HPA; ENSG00000145708; Tissue enhanced (brain, liver).
DR   MIM; 122559; gene.
DR   neXtProt; NX_P24387; -.
DR   OpenTargets; ENSG00000145708; -.
DR   PharmGKB; PA26873; -.
DR   VEuPathDB; HostDB:ENSG00000145708; -.
DR   eggNOG; ENOG502QRNI; Eukaryota.
DR   GeneTree; ENSGT00390000001362; -.
DR   HOGENOM; CLU_056739_0_0_1; -.
DR   InParanoid; P24387; -.
DR   OMA; EFCFPSI; -.
DR   OrthoDB; 5341869at2759; -.
DR   PhylomeDB; P24387; -.
DR   TreeFam; TF105383; -.
DR   PathwayCommons; P24387; -.
DR   Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR   SignaLink; P24387; -.
DR   BioGRID-ORCS; 1393; 8 hits in 1141 CRISPR screens.
DR   ChiTaRS; CRHBP; human.
DR   GeneWiki; CRHBP; -.
DR   GenomeRNAi; 1393; -.
DR   Pharos; P24387; Tbio.
DR   PRO; PR:P24387; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P24387; Protein.
DR   Bgee; ENSG00000145708; Expressed in primordial germ cell in gonad and 114 other cell types or tissues.
DR   ExpressionAtlas; P24387; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0031045; C:dense core granule; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR   GO; GO:0005767; C:secondary lysosome; ISS:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR   GO; GO:0043196; C:varicosity; ISS:UniProtKB.
DR   GO; GO:0051424; F:corticotropin-releasing hormone binding; IDA:UniProtKB.
DR   GO; GO:0042277; F:peptide binding; ISS:UniProtKB.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:UniProtKB.
DR   GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR   GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR   GO; GO:0071314; P:cellular response to cocaine; ISS:UniProtKB.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR   GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR   GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; ISS:UniProtKB.
DR   GO; GO:0035865; P:cellular response to potassium ion; IDA:UniProtKB.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR   GO; GO:0007565; P:female pregnancy; IDA:UniProtKB.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR   GO; GO:0007611; P:learning or memory; TAS:UniProtKB.
DR   GO; GO:0051460; P:negative regulation of corticotropin secretion; IDA:UniProtKB.
DR   GO; GO:1900011; P:negative regulation of corticotropin-releasing hormone receptor activity; IDA:UniProtKB.
DR   GO; GO:0045055; P:regulated exocytosis; IDA:UniProtKB.
DR   GO; GO:0080135; P:regulation of cellular response to stress; IMP:UniProtKB.
DR   GO; GO:0051459; P:regulation of corticotropin secretion; IDA:UniProtKB.
DR   GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; ISS:UniProtKB.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   InterPro; IPR008435; CRF-bd.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR10278; CORTICOTROPIN-RELEASING FACTOR-BINDING PROTEIN; 1.
DR   PANTHER; PTHR10278:SF0; CORTICOTROPIN-RELEASING FACTOR-BINDING PROTEIN; 1.
DR   Pfam; PF05428; CRF-BP; 1.
DR   PIRSF; PIRSF009279; CRF_bd; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   Genevisible; P24387; HS.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT   CHAIN           25..322
FT                   /note="Corticotropin-releasing factor-binding protein"
FT                   /id="PRO_0000020994"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..81
FT                   /evidence="ECO:0000269|PubMed:8307998"
FT   DISULFID        104..141
FT                   /evidence="ECO:0000269|PubMed:8307998"
FT   DISULFID        183..205
FT                   /evidence="ECO:0000269|PubMed:8307998"
FT   DISULFID        237..264
FT                   /evidence="ECO:0000269|PubMed:8307998"
FT   DISULFID        277..318
FT                   /evidence="ECO:0000269|PubMed:8307998"
FT   CONFLICT        279
FT                   /note="N -> D (in Ref. 4; BAD97177)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   322 AA;  36144 MW;  771A894BE06039BD CRC64;
     MSPNFKLQCH FILIFLTALR GESRYLELRE AADYDPFLLF SANLKRELAG EQPYRRALRC
     LDMLSLQGQF TFTADRPQLH CAAFFISEPE EFITIHYDQV SIDCQGGDFL KVFDGWILKG
     EKFPSSQDHP LPSAERYIDF CESGLSRRSI RSSQNVAMIF FRVHEPGNGF TLTIKTDPNL
     FPCNVISQTP NGKFTLVVPH QHRNCSFSII YPVVIKISDL TLGHVNGLQL KKSSAGCEGI
     GDFVELLGGT GLDPSKMTPL ADLCYPFHGP AQMKVGCDNT VVRMVSSGKH VNRVTFEYRQ
     LEPYELENPN GNSIGEFCLS GL
//