EHBP1_MOUSE
ID EHBP1_MOUSE Reviewed; 1231 AA.
AC Q69ZW3; E9QMJ9; Q5SQK3; Q91ZJ6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=EH domain-binding protein 1;
GN Name=Ehbp1; Synonyms=Kiaa0903;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=12174196; DOI=10.1186/1471-2156-3-14;
RA Fuchs S., Resch K., Thiel C., Ulbrich M., Platzer M., Jockusch H.,
RA Schmitt-John T.;
RT "Comparative transcription map of the wobbler critical region on mouse
RT chromosome 11 and the homologous region on human chromosome 2p13-14.";
RL BMC Genet. 3:14-14(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, AND INTERACTION WITH EHD1.
RX PubMed=15247266; DOI=10.1074/jbc.m401918200;
RA Guilherme A., Soriano N.A., Furcinitti P.S., Czech M.P.;
RT "Role of EHD1 and EHBP1 in perinuclear sorting and insulin-regulated GLUT4
RT recycling in 3T3-L1 adipocytes.";
RL J. Biol. Chem. 279:40062-40075(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-174; SER-222;
RP THR-328; SER-335; SER-436; SER-442; SER-446; SER-646 AND SER-765, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in actin reorganization. Links clathrin-
CC mediated endocytosis to the actin cytoskeleton. May act as Rab effector
CC protein and play a role in vesicle trafficking (By similarity).
CC Required for perinuclear sorting and insulin-regulated recycling of
CC SLC2A4/GLUT4 in adipocytes. {ECO:0000250|UniProtKB:Q8NDI1,
CC ECO:0000269|PubMed:15247266}.
CC -!- SUBUNIT: Interacts with EHD1 (PubMed:15247266). Interacts with EHD2.
CC Interacts with RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound
CC forms); at least in case of RAB8A may bind 2 molecules of RAB8A
CC simultaneously through a high and a low affinity binding site,
CC respectively (By similarity). {ECO:0000250|UniProtKB:Q8NDI1,
CC ECO:0000269|PubMed:15247266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NDI1}.
CC Membrane {ECO:0000250|UniProtKB:Q8NDI1}. Endosome
CC {ECO:0000250|UniProtKB:Q8NDI1}. Note=Mostly found in cytosol and plasma
CC membrane. {ECO:0000250|UniProtKB:Q8NDI1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69ZW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZW3-2; Sequence=VSP_024836;
CC -!- DOMAIN: The CAAX motif is a signal for prenylation and required for
CC endosomal colocalization with Rab8 and Rab10.
CC {ECO:0000250|UniProtKB:Q8NDI1}.
CC -!- DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound
CC form). {ECO:0000250|UniProtKB:Q8NDI1}.
CC -!- PTM: Prenylated (Probable). Farnelysation (predominant) and
CC geranylgeranylation has been observed in vitro.
CC {ECO:0000250|UniProtKB:Q8NDI1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32333.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF424697; AAL24806.1; -; mRNA.
DR EMBL; AK173055; BAD32333.1; ALT_INIT; mRNA.
DR EMBL; AL669858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24469.1; -. [Q69ZW3-2]
DR CCDS; CCDS56762.1; -. [Q69ZW3-1]
DR RefSeq; NP_001239444.1; NM_001252515.1. [Q69ZW3-1]
DR RefSeq; NP_694718.4; NM_153078.4. [Q69ZW3-2]
DR AlphaFoldDB; Q69ZW3; -.
DR BMRB; Q69ZW3; -.
DR SMR; Q69ZW3; -.
DR BioGRID; 229762; 9.
DR CORUM; Q69ZW3; -.
DR STRING; 10090.ENSMUSP00000105191; -.
DR iPTMnet; Q69ZW3; -.
DR PhosphoSitePlus; Q69ZW3; -.
DR jPOST; Q69ZW3; -.
DR MaxQB; Q69ZW3; -.
DR PaxDb; Q69ZW3; -.
DR PeptideAtlas; Q69ZW3; -.
DR PRIDE; Q69ZW3; -.
DR ProteomicsDB; 277812; -. [Q69ZW3-1]
DR ProteomicsDB; 277813; -. [Q69ZW3-2]
DR Antibodypedia; 30724; 88 antibodies from 23 providers.
DR DNASU; 216565; -.
DR Ensembl; ENSMUST00000045167; ENSMUSP00000037489; ENSMUSG00000042302. [Q69ZW3-2]
DR Ensembl; ENSMUST00000109563; ENSMUSP00000105191; ENSMUSG00000042302. [Q69ZW3-1]
DR Ensembl; ENSMUST00000180360; ENSMUSP00000136697; ENSMUSG00000042302. [Q69ZW3-2]
DR GeneID; 216565; -.
DR KEGG; mmu:216565; -.
DR UCSC; uc007iea.2; mouse. [Q69ZW3-2]
DR UCSC; uc007ieb.2; mouse. [Q69ZW3-1]
DR CTD; 23301; -.
DR MGI; MGI:2667252; Ehbp1.
DR VEuPathDB; HostDB:ENSMUSG00000042302; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000157597; -.
DR HOGENOM; CLU_004178_1_1_1; -.
DR InParanoid; Q69ZW3; -.
DR OMA; ILMTRRQ; -.
DR OrthoDB; 165311at2759; -.
DR PhylomeDB; Q69ZW3; -.
DR TreeFam; TF105382; -.
DR BioGRID-ORCS; 216565; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ehbp1; mouse.
DR PRO; PR:Q69ZW3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q69ZW3; protein.
DR Bgee; ENSMUSG00000042302; Expressed in floor plate of midbrain and 248 other tissues.
DR ExpressionAtlas; Q69ZW3; baseline and differential.
DR Genevisible; Q69ZW3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR029944; EHBP1.
DR InterPro; IPR019448; NT-C2.
DR PANTHER; PTHR23167:SF43; PTHR23167:SF43; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF10358; NT-C2; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS51840; C2_NT; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Endocytosis; Endosome;
KW Lipoprotein; Membrane; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1231
FT /note="EH domain-binding protein 1"
FT /id="PRO_0000285203"
FT DOMAIN 8..158
FT /note="C2 NT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01186"
FT DOMAIN 453..558
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1059..1212
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 266..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..219
FT /evidence="ECO:0000255"
FT COILED 812..882
FT /evidence="ECO:0000255"
FT COILED 1032..1100
FT /evidence="ECO:0000255"
FT COILED 1136..1230
FT /evidence="ECO:0000255"
FT MOTIF 1228..1231
FT /note="CAAX motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NDI1"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDI1"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDI1"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDI1"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDI1"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDI1"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDI1"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NDI1"
FT VAR_SEQ 288..312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12174196"
FT /id="VSP_024836"
FT CONFLICT 46..47
FT /note="RR -> KE (in Ref. 1; AAL24806)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="K -> R (in Ref. 1; AAL24806)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="S -> N (in Ref. 2; BAD32333)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="T -> A (in Ref. 1; AAL24806)"
FT /evidence="ECO:0000305"
FT CONFLICT 999
FT /note="A -> G (in Ref. 1; AAL24806)"
FT /evidence="ECO:0000305"
FT CONFLICT 1089
FT /note="D -> G (in Ref. 1; AAL24806)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="E -> A (in Ref. 1; AAL24806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1231 AA; 139104 MW; E23307E35621A7A2 CRC64;
MASVWKRLQR VGKHASKFQF VASYQELMVE CTKKWQPDKL VVVWTRRSRR KSSKAHSWQP
GIKNPYRGVV VWPVPENIEI TVTLFKDPHA EEFEDKEWTF VIENESPSGR RKALATSSIN
MKQYASPMPT QTDVKLKFKP LSKKVVSATL QFSLSCIFLR EGKATDEDMQ SLASLMSMKQ
ADIGNLDDFE EDNEDDDENR VNQEEKAAKI TEIVNQLNAL SSLDEDQDDC IKQANVPSAK
SASSSEELIN TLNFLDEAQK DLATVNTNPF DEPDVTELNP FGDPDSEEPI TETTSPKKPE
ESFYNNSCNP FKGVQTPQYL NPFDEPETFV MIKDSPPQST RRKNLRPVDM SKYLYADSSK
SEEELDESNP FYEPKPTSPN NLVNTVQEGE TERRVKRRAP APPAPLAPPA PPAPPALTPK
TGVNENTVVS AGKDLSTSPK PSPIPSPVLG QKPNASQSLL AWCREVTKNY RGVKITNFTT
SWRNGLSFCA ILHHFRPDLI DYKSLNPQDI KENNKKAYDG FASIGISRLL EPSDMVLLAI
PDKLTVMTYL YQIRAHFSGQ ELNVVQIEEN SSKSTYKVGN YETDTNSSVD QEKFYAELSD
LKREPEPHQP ARGAVDLLSQ DDSVFVTDSG VGESESEHQT PDDHLSPSTA SPYYRRTKSD
TEPQKSQQSS ARTSGSDDPG LSSSTDSAQA LASLGKKRLK AENLELSDLC VSDKKKDVSP
LSAYEQKLQT VHASSDMEQG KMEKSRSLEC RLDGELAITK PNVSSPSKLG YNRDTDFTKK
PCASLRQIES DPDADKSTLN HADHPNKAVQ HRMLSRQEEL KERARVLLEQ ARRDAAFKVG
SKHGGSAAPA LCSRQLNDQQ DEERRRQLRE RARQLIAEAR CGVKMSELPS YGEMAAEKLK
ERSKASGDEN DNIEIDTNEE IPEGFVVGGG DELTNIESDL DNPEQNSKVV DLRLKKLLEA
QPQVANLLPS AAQKAVTEAS EQGEKSGVED LRTERLQKAT ERFRNPVVFN KDSTVRKTQL
QSFSQYVENR PEMKRQRSIQ EDTKRGTEEK AEITETQRKP SEDEKGFKDT SQYVVGELAA
LENEQKQIDT RAALVEKRLR YLMDTGRNTE EEEAMMQEWF MLVNKKNALI RRMNQLSLLE
KEHDLERRYE LLNRELRAML AIEDWQKTEA QKRREQLLLD ELVALVDKRD ALVRDLDAQE
KQAEEEDEHL ERTLEQNKGK MAKKEEKCAL Q
