DNMBP_HUMAN
ID DNMBP_HUMAN Reviewed; 1577 AA.
AC Q6XZF7; Q8IVY3; Q9Y2L3;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Dynamin-binding protein {ECO:0000312|HGNC:HGNC:30373};
DE AltName: Full=Scaffold protein Tuba {ECO:0000305|PubMed:14506234};
GN Name=DNMBP {ECO:0000312|HGNC:HGNC:30373};
GN Synonyms=ARHGEF36 {ECO:0000312|HGNC:HGNC:30373},
GN KIAA1010 {ECO:0000303|PubMed:10231032}, TUBA {ECO:0000303|PubMed:14506234};
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] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=14506234; DOI=10.1074/jbc.m308104200;
RA Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT domains, links dynamin to regulation of the actin cytoskeleton.";
RL J. Biol. Chem. 278:49031-49043(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-1577 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT TRP-1413.
RC TISSUE=Uterus;
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 [4]
RP INTERACTION WITH TJP1 AND WASL, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17015620; DOI=10.1083/jcb.200605012;
RA Otani T., Ichii T., Aono S., Takeichi M.;
RT "Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial
RT cells.";
RL J. Cell Biol. 175:135-146(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [7]
RP FUNCTION, INTERACTION WITH WASL, INTERACTION WITH L.MONOCYTOGENES INLC, AND
RP SUBUNIT (MICROBIAL INFECTION).
RX PubMed=19767742; DOI=10.1038/ncb1964;
RA Rajabian T., Gavicherla B., Heisig M., Mueller-Altrock S., Goebel W.,
RA Gray-Owen S.D., Ireton K.;
RT "The bacterial virulence factor InlC perturbs apical cell junctions and
RT promotes cell-to-cell spread of Listeria.";
RL Nat. Cell Biol. 11:1212-1218(2009).
RN [8]
RP FUNCTION.
RX PubMed=20479467; DOI=10.1083/jcb.201002097;
RA Qin Y., Meisen W.H., Hao Y., Macara I.G.;
RT "Tuba, a Cdc42 GEF, is required for polarized spindle orientation during
RT epithelial cyst formation.";
RL J. Cell Biol. 189:661-669(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND SER-684, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP VARIANT CTRCT48 271-ARG--THR-1577 DEL, AND INVOLVEMENT IN CTRCT48.
RX PubMed=30290152; DOI=10.1016/j.ajhg.2018.09.004;
RA Ansar M., Chung H.L., Taylor R.L., Nazir A., Imtiaz S., Sarwar M.T.,
RA Manousopoulou A., Makrythanasis P., Saeed S., Falconnet E., Guipponi M.,
RA Pournaras C.J., Ansari M.A., Ranza E., Santoni F.A., Ahmed J., Shah I.,
RA Gul K., Black G.C., Bellen H.J., Antonarakis S.E.;
RT "Bi-allelic loss-of-function variants in DNMBP cause infantile cataracts.";
RL Am. J. Hum. Genet. 103:568-578(2018).
RN [15]
RP STRUCTURE BY NMR OF 1278-1353 AND 1510-1575.
RG RIKEN structural genomics initiative (RSGI);
RT "NMR structure of SH3 domain of hypothetical protein BAA76854.1.";
RL Submitted (DEC-2003) to the PDB data bank.
RN [16] {ECO:0007744|PDB:1UHC}
RP STRUCTURE BY NMR OF 1510-1575.
RA Abe T., Hirota H., Kobayashi N., Hayashi F., Yokoyama S.;
RT "Solution structure of RSGI RUH-002, a SH3 domain of KIAA1010 protein [Homo
RT sapiens].";
RL Submitted (JUN-2003) to the PDB data bank.
RN [17] {ECO:0007744|PDB:4GLM}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 246-301.
RA Guan X., Dong A., Huang H., Tempel W., Gu J., Sidhu S., Bountra C.,
RA Arrowsmith C.H., Edwards A.M., Tong Y.;
RT "Crystal structure of the SH3 Domain of DNMBP protein [Homo sapiens].";
RL Submitted (AUG-2012) to the PDB data bank.
RN [18] {ECO:0007744|PDB:4CC2, ECO:0007744|PDB:4CC3, ECO:0007744|PDB:4CC4, ECO:0007744|PDB:4CC7}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1513-1577 IN COMPLEX WITH WASL;
RP MURINE ENAH AND L.MONOCYTOGENES INLC, SUBUNIT, AND MUTAGENESIS OF VAL-1521;
RP PRO-1529 AND ASN-1569.
RX PubMed=24332715; DOI=10.1016/j.str.2013.10.017;
RA Polle L., Rigano L.A., Julian R., Ireton K., Schubert W.D.;
RT "Structural details of human tuba recruitment by InlC of Listeria
RT monocytogenes elucidate bacterial cell-cell spreading.";
RL Structure 22:304-314(2014).
CC -!- FUNCTION: Plays a critical role as a guanine nucleotide exchange factor
CC (GEF) for CDC42 in several intracellular processes associated with the
CC actin and microtubule cytoskeleton. Regulates the structure of apical
CC junctions through F-actin organization in epithelial cells
CC (PubMed:19767742, PubMed:17015620). Participates in the normal
CC lumenogenesis of epithelial cell cysts by regulating spindle
CC orientation (PubMed:20479467). Plays a role in ciliogenesis (By
CC similarity). May play a role in membrane trafficking between the cell
CC surface and the Golgi (By similarity). {ECO:0000250|UniProtKB:E2RP94,
CC ECO:0000250|UniProtKB:Q6TXD4, ECO:0000269|PubMed:17015620,
CC ECO:0000269|PubMed:19767742, ECO:0000269|PubMed:20479467}.
CC -!- SUBUNIT: Binds DNM1 via its N-terminal SH3 domains. The C-terminal SH3
CC domain binds a complex containing actin, tubulin, Hsp70 and actin-
CC regulatory proteins, such as ENAH, EVL, WIRE, CR16, WAVE1 and NAP1L1
CC (By similarity). Interacts with FASLG (PubMed:19807924). Interacts (via
CC SH3 domain 6) with WASL (PubMed:19767742, PubMed:24332715,
CC PubMed:17015620). Interacts (via SH3 domain 6) interacts with ENAH
CC (PubMed:24332715). Interacts (via C-terminal domain) with TJP1;
CC required for the apical cell-cell junction localization of DNMBP
CC (PubMed:17015620). {ECO:0000250, ECO:0000250|UniProtKB:Q6TXD4,
CC ECO:0000269|PubMed:17015620, ECO:0000269|PubMed:19767742,
CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:24332715}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via SH3 domain 6) with
CC L.monocytogenes InlC. {ECO:0000269|PubMed:19767742,
CC ECO:0000269|PubMed:24332715}.
CC -!- INTERACTION:
CC Q6XZF7; Q9NQY0: BIN3; NbExp=2; IntAct=EBI-2483419, EBI-2653038;
CC Q6XZF7; P21575: Dnm1; Xeno; NbExp=3; IntAct=EBI-2483419, EBI-80070;
CC Q6XZF7-1; O00401: WASL; NbExp=2; IntAct=EBI-16085546, EBI-957615;
CC Q6XZF7-1; Q03173-1: Enah; Xeno; NbExp=2; IntAct=EBI-16085546, EBI-16085647;
CC Q6XZF7-1; P71451: inlC; Xeno; NbExp=6; IntAct=EBI-16085546, EBI-21019720;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17015620}. Golgi
CC apparatus, Golgi stack {ECO:0000250|UniProtKB:Q6TXD4}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q6TXD4}. Synapse
CC {ECO:0000250|UniProtKB:M0R4F8}. Cell junction
CC {ECO:0000269|PubMed:17015620}. Note=Localizes to the apical junction,
CC colocalizes with TJP1. {ECO:0000269|PubMed:17015620}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6XZF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6XZF7-2; Sequence=VSP_012079;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, skeletal
CC muscle, kidney and pancreas. {ECO:0000269|PubMed:14506234}.
CC -!- DISEASE: Cataract 48 (CTRCT48) [MIM:618415]: A form of cataract, an
CC opacification of the crystalline lens of the eye that frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function. CTRCT48 is
CC an autosomal recessive form characterized by infantile or early-
CC childhood onset. {ECO:0000269|PubMed:30290152}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
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DR EMBL; AY196211; AAP34307.1; -; mRNA.
DR EMBL; AB023227; BAA76854.1; -; mRNA.
DR EMBL; BC041628; AAH41628.1; -; mRNA.
DR CCDS; CCDS7485.1; -. [Q6XZF7-1]
DR RefSeq; NP_001305255.1; NM_001318326.1.
DR RefSeq; NP_001305256.1; NM_001318327.1.
DR RefSeq; NP_056036.1; NM_015221.3. [Q6XZF7-1]
DR RefSeq; XP_011537861.1; XM_011539559.2. [Q6XZF7-1]
DR PDB; 1UG1; NMR; -; A=1278-1355.
DR PDB; 1UHC; NMR; -; A=1510-1575.
DR PDB; 4CC2; X-ray; 1.55 A; A/C=1513-1577.
DR PDB; 4CC3; X-ray; 1.97 A; A/C/E/G=1513-1577.
DR PDB; 4CC4; X-ray; 2.60 A; B/D/F=1513-1577.
DR PDB; 4CC7; X-ray; 1.97 A; A/C/E/G/I/K/M=1513-1577.
DR PDB; 4GLM; X-ray; 1.90 A; A/B/C/D=246-301.
DR PDBsum; 1UG1; -.
DR PDBsum; 1UHC; -.
DR PDBsum; 4CC2; -.
DR PDBsum; 4CC3; -.
DR PDBsum; 4CC4; -.
DR PDBsum; 4CC7; -.
DR PDBsum; 4GLM; -.
DR AlphaFoldDB; Q6XZF7; -.
DR SMR; Q6XZF7; -.
DR BioGRID; 116869; 113.
DR DIP; DIP-53822N; -.
DR IntAct; Q6XZF7; 32.
DR MINT; Q6XZF7; -.
DR STRING; 9606.ENSP00000315659; -.
DR ChEMBL; CHEMBL4295871; -.
DR iPTMnet; Q6XZF7; -.
DR MetOSite; Q6XZF7; -.
DR PhosphoSitePlus; Q6XZF7; -.
DR BioMuta; DNMBP; -.
DR DMDM; 56404535; -.
DR EPD; Q6XZF7; -.
DR jPOST; Q6XZF7; -.
DR MassIVE; Q6XZF7; -.
DR MaxQB; Q6XZF7; -.
DR PaxDb; Q6XZF7; -.
DR PeptideAtlas; Q6XZF7; -.
DR PRIDE; Q6XZF7; -.
DR ProteomicsDB; 67829; -. [Q6XZF7-1]
DR ProteomicsDB; 67830; -. [Q6XZF7-2]
DR ABCD; Q6XZF7; 6 sequenced antibodies.
DR Antibodypedia; 31117; 154 antibodies from 25 providers.
DR DNASU; 23268; -.
DR Ensembl; ENST00000324109.9; ENSP00000315659.4; ENSG00000107554.17. [Q6XZF7-1]
DR GeneID; 23268; -.
DR KEGG; hsa:23268; -.
DR MANE-Select; ENST00000324109.9; ENSP00000315659.4; NM_015221.4; NP_056036.1.
DR UCSC; uc001kqg.3; human. [Q6XZF7-1]
DR CTD; 23268; -.
DR DisGeNET; 23268; -.
DR GeneCards; DNMBP; -.
DR HGNC; HGNC:30373; DNMBP.
DR HPA; ENSG00000107554; Low tissue specificity.
DR MalaCards; DNMBP; -.
DR MIM; 611282; gene.
DR MIM; 618415; phenotype.
DR neXtProt; NX_Q6XZF7; -.
DR OpenTargets; ENSG00000107554; -.
DR Orphanet; 98994; Total early-onset cataract.
DR PharmGKB; PA134950706; -.
DR VEuPathDB; HostDB:ENSG00000107554; -.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00950000183088; -.
DR HOGENOM; CLU_252350_0_0_1; -.
DR InParanoid; Q6XZF7; -.
DR OrthoDB; 207472at2759; -.
DR PhylomeDB; Q6XZF7; -.
DR TreeFam; TF330015; -.
DR PathwayCommons; Q6XZF7; -.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; Q6XZF7; -.
DR SIGNOR; Q6XZF7; -.
DR BioGRID-ORCS; 23268; 14 hits in 1078 CRISPR screens.
DR ChiTaRS; DNMBP; human.
DR EvolutionaryTrace; Q6XZF7; -.
DR GenomeRNAi; 23268; -.
DR Pharos; Q6XZF7; Tbio.
DR PRO; PR:Q6XZF7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q6XZF7; protein.
DR Bgee; ENSG00000107554; Expressed in jejunal mucosa and 199 other tissues.
DR ExpressionAtlas; Q6XZF7; baseline and differential.
DR Genevisible; Q6XZF7; HS.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11798; SH3_DNMBP_C1; 1.
DR CDD; cd11794; SH3_DNMBP_N1; 1.
DR CDD; cd11795; SH3_DNMBP_N2; 1.
DR CDD; cd11796; SH3_DNMBP_N3; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR035469; DNMBP.
DR InterPro; IPR035820; DNMBP_SH3_C1.
DR InterPro; IPR035817; DNMBP_SH3_N1.
DR InterPro; IPR035818; DNMBP_SH3_N2.
DR InterPro; IPR035819; DNMBP_SH3_N3.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22834:SF19; PTHR22834:SF19; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 6.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 6.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cataract; Cell junction;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Synapse.
FT CHAIN 1..1577
FT /note="Dynamin-binding protein"
FT /id="PRO_0000079959"
FT DOMAIN 2..61
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 66..126
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 145..204
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 243..302
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 784..967
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1008..1217
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 1285..1348
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1513..1576
FT /note="SH3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 211..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 693..757
FT /evidence="ECO:0000255"
FT COILED 1136..1173
FT /evidence="ECO:0000255"
FT COMPBIAS 335..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..754
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012079"
FT VARIANT 81
FT /note="E -> D (in dbSNP:rs12267912)"
FT /id="VAR_050955"
FT VARIANT 271..1577
FT /note="Missing (in CTRCT48)"
FT /evidence="ECO:0000269|PubMed:30290152"
FT /id="VAR_081450"
FT VARIANT 373
FT /note="N -> K (in dbSNP:rs35924554)"
FT /id="VAR_050956"
FT VARIANT 914
FT /note="N -> K (in dbSNP:rs7919507)"
FT /id="VAR_050957"
FT VARIANT 1413
FT /note="C -> W (in dbSNP:rs11190305)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024339"
FT MUTAGEN 1521
FT /note="V->R: Decreased interaction of SH3 domain 6 with
FT L.monocytogenes InlC."
FT /evidence="ECO:0000269|PubMed:24332715"
FT MUTAGEN 1529
FT /note="P->A: Wild-type interaction of SH3 domain 6 with
FT L.monocytogenes InlC."
FT /evidence="ECO:0000269|PubMed:24332715"
FT MUTAGEN 1569
FT /note="N->R: Decreased interaction of SH3 domain 6 with
FT L.monocytogenes InlC."
FT /evidence="ECO:0000269|PubMed:24332715"
FT CONFLICT 831
FT /note="M -> T (in Ref. 3; AAH41628)"
FT /evidence="ECO:0000305"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:4GLM"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:4GLM"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:4GLM"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4GLM"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4GLM"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:4GLM"
FT HELIX 1278..1283
FT /evidence="ECO:0007829|PDB:1UG1"
FT HELIX 1286..1288
FT /evidence="ECO:0007829|PDB:1UG1"
FT STRAND 1289..1294
FT /evidence="ECO:0007829|PDB:1UG1"
FT STRAND 1300..1302
FT /evidence="ECO:0007829|PDB:1UG1"
FT STRAND 1311..1317
FT /evidence="ECO:0007829|PDB:1UG1"
FT STRAND 1324..1330
FT /evidence="ECO:0007829|PDB:1UG1"
FT STRAND 1332..1339
FT /evidence="ECO:0007829|PDB:1UG1"
FT HELIX 1340..1342
FT /evidence="ECO:0007829|PDB:1UG1"
FT STRAND 1343..1345
FT /evidence="ECO:0007829|PDB:1UG1"
FT STRAND 1517..1522
FT /evidence="ECO:0007829|PDB:4CC2"
FT STRAND 1528..1531
FT /evidence="ECO:0007829|PDB:1UHC"
FT STRAND 1539..1546
FT /evidence="ECO:0007829|PDB:4CC2"
FT STRAND 1554..1559
FT /evidence="ECO:0007829|PDB:4CC2"
FT STRAND 1562..1567
FT /evidence="ECO:0007829|PDB:4CC2"
FT HELIX 1568..1570
FT /evidence="ECO:0007829|PDB:4CC2"
FT STRAND 1571..1574
FT /evidence="ECO:0007829|PDB:4CC2"
SQ SEQUENCE 1577 AA; 177347 MW; 5A1FDCB06124F627 CRC64;
MEAGSVVRAI FDFCPSVSEE LPLFVGDIIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEIVT
IPSLKEGERL FVCICEFTSQ ELDNLPLHRG DLVILDGIPT AGWLQGRSCW GARGFFPSSC
VRELCLSSQS RQWHSQSALF QIPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP
GWFEGELEGR RGIFPEGFVE LLGPLRTVDE SVSSGNQDDC IVNGEVDTPV GEEEIGPDED
EEEPGTYGVA LYRFQALEPN ELDFEVGDKI RILATLEDGW LEGSLKGRTG IFPYRFVKLC
PDTRVEETMA LPQEGSLARI PETSLDCLEN TLGVEEQRHE TSDHEAEEPD CIISEAPTSP
LGHLTSEYDT DRNSYQDEDT AGGPPRSPGV EWEMPLATDS PTSDPTEVVN GISSQPQVPF
HPNLQKSQYY STVGGSHPHS EQYPDLLPLE ARTRDYASLP PKRMYSQLKT LQKPVLPLYR
GSSVSASRVV KPRQSSPQLH NLASYTKKHH TSSVYSISER LEMKPGPQAQ GLVMEAATHS
QGDGSTDLDS KLTQQLIEFE KSLAGPGTEP DKILRHFSIM DFNSEKDIVR GSSKLITEQE
LPERRKALRP PPPRPCTPVS TSPHLLVDQN LKPAPPLVVR PSRPAPLPPS AQQRTNAVSP
KLLSRHRPTC ETLEKEGPGH MGRSLDQTSP CPLVLVRIEE MERDLDMYSR AQEELNLMLE
EKQDESSRAE TLEDLKFCES NIESLNMELQ QLREMTLLSS QSSSLVAPSG SVSAENPEQR
MLEKRAKVIE ELLQTERDYI RDLEMCIERI MVPMQQAQVP NIDFEGLFGN MQMVIKVSKQ
LLAALEISDA VGPVFLGHRD ELEGTYKIYC QNHDEAIALL EIYEKDEKIQ KHLQDSLADL
KSLYNEWGCT NYINLGSFLI KPVQRVMRYP LLLMELLNST PESHPDKVPL TNAVLAVKEI
NVNINEYKRR KDLVLKYRKG DEDSLMEKIS KLNIHSIIKK SNRVSSHLKH LTGFAPQIKD
EVFEETEKNF RMQERLIKSF IRDLSLYLQH IRESACVKVV AAVSMWDVCM ERGHRDLEQF
ERVHRYISDQ LFTNFKERTE RLVISPLNQL LSMFTGPHKL VQKRFDKLLD FYNCTERAEK
LKDKKTLEEL QSARNNYEAL NAQLLDELPK FHQYAQGLFT NCVHGYAEAH CDFVHQALEQ
LKPLLSLLKV AGREGNLIAI FHEEHSRVLQ QLQVFTFFPE SLPATKKPFE RKTIDRQSAR
KPLLGLPSYM LQSEELRASL LARYPPEKLF QAERNFNAAQ DLDVSLLEGD LVGVIKKKDP
MGSQNRWLID NGVTKGFVYS SFLKPYNPRR SHSDASVGSH SSTESEHGSS SPRFPRQNSG
STLTFNPSSM AVSFTSGSCQ KQPQDASPPP KECDQGTLSA SLNPSNSESS PSRCPSDPDS
TSQPRSGDSA DVARDVKQPT ATPRSYRNFR HPEIVGYSVP GRNGQSQDLV KGCARTAQAP
EDRSTEPDGS EAEGNQVYFA VYTFKARNPN ELSVSANQKL KILEFKDVTG NTEWWLAEVN
GKKGYVPSNY IRKTEYT
