ACAP1_HUMAN
ID ACAP1_HUMAN Reviewed; 740 AA.
AC Q15027; Q53XN9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1;
DE AltName: Full=Centaurin-beta-1;
DE Short=Cnt-b1;
GN Name=ACAP1; Synonyms=CENTB1, KIAA0050;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ARG-448.
RX PubMed=11062263; DOI=10.1083/jcb.151.3.627;
RA Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., Hsu V.W.,
RA Donaldson J.G., Randazzo P.A.;
RT "ACAPs are arf6 GTPase-activating proteins that function in the cell
RT periphery.";
RL J. Cell Biol. 151:627-638(2000).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT SER-554, IDENTIFICATION BY MASS SPECTROMETRY,
RP INTERACTION WITH ITGB1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-14;
RP SER-29; SER-277; THR-289; SER-358; THR-389; THR-461; SER-554; SER-568;
RP THR-711; TYR-712 AND SER-724.
RX PubMed=16256741; DOI=10.1016/j.devcel.2005.09.012;
RA Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.;
RT "Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent
RT recycling of integrin beta1 to control cell migration.";
RL Dev. Cell 9:663-673(2005).
RN [6]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-485, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary adenoma;
RX PubMed=16777052; DOI=10.1016/j.ab.2006.05.024;
RA Zhan X., Desiderio D.M.;
RT "Nitroproteins from a human pituitary adenoma tissue discovered with a
RT nitrotyrosine affinity column and tandem mass spectrometry.";
RL Anal. Biochem. 354:279-289(2006).
RN [7]
RP INTERACTION WITH PHOSPHOLIPIDS, AND MUTAGENESIS OF LYS-274.
RX PubMed=17010122; DOI=10.1111/j.1600-0854.2006.00480.x;
RA Shinozaki-Narikawa N., Kodama T., Shibasaki Y.;
RT "Cooperation of phosphoinositides and BAR domain proteins in endosomal
RT tubulation.";
RL Traffic 7:1539-1550(2006).
RN [8]
RP FUNCTION, INTERACTION WITH GULP AND ARF6, AND MUTAGENESIS OF ARG-448.
RX PubMed=17398097; DOI=10.1016/j.cub.2007.03.014;
RA Ma Z., Nie Z., Luo R., Casanova J.E., Ravichandran K.S.;
RT "Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing
RT adaptor protein GULP.";
RL Curr. Biol. 17:722-727(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH CLTC.
RX PubMed=17664335; DOI=10.1083/jcb.200608033;
RA Li J., Peters P.J., Bai M., Dai J., Bos E., Kirchhausen T., Kandror K.V.,
RA Hsu V.W.;
RT "An ACAP1-containing clathrin coat complex for endocytic recycling.";
RL J. Cell Biol. 178:453-464(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 378-740 WILD TYPE AND MUTANT
RP ASP-554 IN COMPLEX WITH ITGB1 PEPTIDE AND ZINC IONS, FUNCTION, INTERACTION
RP WITH ITGB1, AND MUTAGENESIS OF SER-554.
RX PubMed=22645133; DOI=10.1074/jbc.m112.378810;
RA Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F., Hsu V.W.;
RT "Mechanistic insights into regulated cargo binding by ACAP1 protein.";
RL J. Biol. Chem. 287:28675-28685(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-377, STRUCTURE BY ELECTRON
RP MICROSCOPY (12.0 ANGSTROMS) OF 1-377, SUBUNIT, BAR DOMAIN, PH DOMAIN, AND
RP MUTAGENESIS OF PHE-280.
RX PubMed=25284369; DOI=10.1016/j.devcel.2014.08.020;
RA Pang X., Fan J., Zhang Y., Zhang K., Gao B., Ma J., Li J., Deng Y.,
RA Zhou Q., Egelman E.H., Hsu V.W., Sun F.;
RT "A PH domain in ACAP1 possesses key features of the BAR domain in promoting
RT membrane curvature.";
RL Dev. Cell 31:73-86(2014).
RN [12]
RP VARIANTS [LARGE SCALE ANALYSIS] ARG-114 AND GLN-129.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC (ARF6) required for clathrin-dependent export of proteins from
CC recycling endosomes to trans-Golgi network and cell surface. Required
CC for regulated export of ITGB1 from recycling endosomes to the cell
CC surface and ITGB1-dependent cell migration.
CC {ECO:0000269|PubMed:11062263, ECO:0000269|PubMed:16256741,
CC ECO:0000269|PubMed:17398097, ECO:0000269|PubMed:17664335,
CC ECO:0000269|PubMed:22645133}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC {ECO:0000269|PubMed:11062263}.
CC -!- SUBUNIT: Banana-shaped homodimer laterally assembling into tetramers,
CC the tetramers further pack helically onto the membrane. Interacts with
CC GTP-bound ARF6. Interacts with third cytoplasmic loop of SLC2A4/GLUT4.
CC Interacts with CLTC. Interacts with GULP1. Forms a complex with GDP-
CC bound ARF6 and GULP1. Interacts with ITGB1; required for ITGB1
CC recycling. {ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:17010122,
CC ECO:0000269|PubMed:17398097, ECO:0000269|PubMed:17664335,
CC ECO:0000269|PubMed:22645133, ECO:0000269|PubMed:25284369}.
CC -!- INTERACTION:
CC Q15027; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-751746, EBI-11958845;
CC Q15027; P62993: GRB2; NbExp=3; IntAct=EBI-751746, EBI-401755;
CC Q15027; Q92993: KAT5; NbExp=3; IntAct=EBI-751746, EBI-399080;
CC Q15027; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-751746, EBI-11742507;
CC Q15027; O76041: NEBL; NbExp=3; IntAct=EBI-751746, EBI-2880203;
CC Q15027; P17252: PRKCA; NbExp=3; IntAct=EBI-751746, EBI-1383528;
CC Q15027; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-751746, EBI-9090795;
CC Q15027; P14927: UQCRB; NbExp=3; IntAct=EBI-751746, EBI-743128;
CC Q15027; P22695: UQCRC2; NbExp=3; IntAct=EBI-751746, EBI-1051424;
CC Q15027; P61981: YWHAG; NbExp=3; IntAct=EBI-751746, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:16256741}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16256741}; Cytoplasmic side
CC {ECO:0000269|PubMed:16256741}.
CC -!- TISSUE SPECIFICITY: Highest level in lung and spleen. Low level in
CC heart, kidney, liver and pancreas. {ECO:0000269|PubMed:11062263}.
CC -!- DOMAIN: PH domain binds phospholipids including phosphatidic acid,
CC phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate
CC (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate
CC ACAP1-binding to PIP2 or PIP3 containing membranes. Only one PH domain
CC of one ACAP1 dimer inserts into the membrane, while the other PH domain
CC acts primaryly to interact with adjacent ACAP1 dimers.
CC {ECO:0000269|PubMed:25284369}.
CC -!- DOMAIN: The BAR domain mediates homodimerization, it can neither bind
CC membrane nor impart curvature, but instead requires the neighboring PH
CC domain to achieve these functions. {ECO:0000269|PubMed:25284369}.
CC -!- PTM: Phosphorylation at Ser-554 by PKB is required for interaction with
CC ITGB1, export of ITGB1 from recycling endosomes to the cell surface and
CC ITGB1-dependent cell migration. {ECO:0000269|PubMed:16256741}.
CC -!- MISCELLANEOUS: Cells overexpressing ACAP1 show an accumulation of ITGB1
CC in recycling endosomes and inhibition of stimulation-dependent cell
CC migration. Cells with reduced levels of ACAP1 or AKT1 and AKT2 show
CC inhibition of stimulation-dependent cell migration. Cells
CC overexpressing ACAP1 and PIP5K1C show formation of tubular structures
CC derived from endosomal membranes.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06418.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D30758; BAA06418.2; ALT_INIT; mRNA.
DR EMBL; BT009788; AAP88790.1; -; mRNA.
DR EMBL; BC018543; AAH18543.1; -; mRNA.
DR CCDS; CCDS11101.1; -.
DR RefSeq; NP_055531.1; NM_014716.3.
DR PDB; 3JUE; X-ray; 2.30 A; A/B=378-740.
DR PDB; 3T9K; X-ray; 2.30 A; A/B=378-740.
DR PDB; 4CKG; EM; 12.00 A; A/B/C/D=1-377.
DR PDB; 4CKH; EM; 14.00 A; A/B/C/D=1-377.
DR PDB; 4F1P; X-ray; 2.30 A; A/B=378-740.
DR PDB; 4NSW; X-ray; 2.20 A; A/B=1-377.
DR PDB; 5H3D; EM; 14.00 A; A/B/C/D=1-377.
DR PDBsum; 3JUE; -.
DR PDBsum; 3T9K; -.
DR PDBsum; 4CKG; -.
DR PDBsum; 4CKH; -.
DR PDBsum; 4F1P; -.
DR PDBsum; 4NSW; -.
DR PDBsum; 5H3D; -.
DR AlphaFoldDB; Q15027; -.
DR SMR; Q15027; -.
DR BioGRID; 115092; 14.
DR CORUM; Q15027; -.
DR IntAct; Q15027; 17.
DR MINT; Q15027; -.
DR STRING; 9606.ENSP00000158762; -.
DR GlyGen; Q15027; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q15027; -.
DR PhosphoSitePlus; Q15027; -.
DR BioMuta; ACAP1; -.
DR DMDM; 3183210; -.
DR EPD; Q15027; -.
DR jPOST; Q15027; -.
DR MassIVE; Q15027; -.
DR MaxQB; Q15027; -.
DR PaxDb; Q15027; -.
DR PeptideAtlas; Q15027; -.
DR PRIDE; Q15027; -.
DR ProteomicsDB; 60378; -.
DR Antibodypedia; 24069; 249 antibodies from 34 providers.
DR DNASU; 9744; -.
DR Ensembl; ENST00000158762.8; ENSP00000158762.3; ENSG00000072818.12.
DR Ensembl; ENST00000672212.1; ENSP00000499859.1; ENSG00000288169.1.
DR GeneID; 9744; -.
DR KEGG; hsa:9744; -.
DR MANE-Select; ENST00000158762.8; ENSP00000158762.3; NM_014716.4; NP_055531.1.
DR UCSC; uc002ggd.3; human.
DR CTD; 9744; -.
DR DisGeNET; 9744; -.
DR GeneCards; ACAP1; -.
DR HGNC; HGNC:16467; ACAP1.
DR HPA; ENSG00000072818; Tissue enhanced (bone marrow, intestine, lymphoid tissue).
DR MIM; 607763; gene.
DR neXtProt; NX_Q15027; -.
DR OpenTargets; ENSG00000072818; -.
DR PharmGKB; PA26406; -.
DR VEuPathDB; HostDB:ENSG00000072818; -.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000160289; -.
DR HOGENOM; CLU_012513_0_0_1; -.
DR InParanoid; Q15027; -.
DR OMA; QATYFQQ; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q15027; -.
DR TreeFam; TF318315; -.
DR PathwayCommons; Q15027; -.
DR SignaLink; Q15027; -.
DR SIGNOR; Q15027; -.
DR BioGRID-ORCS; 9744; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; ACAP1; human.
DR EvolutionaryTrace; Q15027; -.
DR GeneWiki; CENTB1; -.
DR GenomeRNAi; 9744; -.
DR Pharos; Q15027; Tbio.
DR PRO; PR:Q15027; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q15027; protein.
DR Bgee; ENSG00000072818; Expressed in granulocyte and 92 other tissues.
DR ExpressionAtlas; Q15027; baseline and differential.
DR Genevisible; Q15027; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23180; PTHR23180; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Endosome; GTPase activation; Membrane;
KW Metal-binding; Nitration; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
FT CHAIN 1..740
FT /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT containing protein 1"
FT /id="PRO_0000074209"
FT DOMAIN 1..226
FT /note="BAR"
FT DOMAIN 265..360
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 405..527
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 606..635
FT /note="ANK 1"
FT REPEAT 639..668
FT /note="ANK 2"
FT REPEAT 672..702
FT /note="ANK 3"
FT ZN_FING 420..443
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 1..382
FT /note="Required for formation of endosomal tubules when
FT overexpressed with PIP5K1C"
FT REGION 405..740
FT /note="Required for interaction with GULP1"
FT REGION 525..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..566
FT /note="Prevents interaction with ITGB1 when S-554 is not
FT phosphorylated"
FT MOD_RES 485
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16777052"
FT MOD_RES 554
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000269|PubMed:16256741"
FT VARIANT 68
FT /note="R -> C (in dbSNP:rs35933585)"
FT /id="VAR_048328"
FT VARIANT 114
FT /note="K -> R (in a breast cancer sample; somatic mutation;
FT dbSNP:rs759855054)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036178"
FT VARIANT 129
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs754740225)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036179"
FT VARIANT 533
FT /note="R -> W (in dbSNP:rs35019942)"
FT /id="VAR_048329"
FT MUTAGEN 14
FT /note="S->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 29
FT /note="S->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 274
FT /note="K->N: Loss of binding to PIP2 and PIP3. Loss of
FT association with endosomal tubules when coexpressed with
FT PIP5K1C."
FT /evidence="ECO:0000269|PubMed:17010122"
FT MUTAGEN 277
FT /note="S->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 280
FT /note="F->A: Reduced membrane binding and ability to induce
FT liposome tubulation."
FT /evidence="ECO:0000269|PubMed:25284369"
FT MUTAGEN 280
FT /note="F->E: Almost abolishes membrane binding."
FT /evidence="ECO:0000269|PubMed:25284369"
FT MUTAGEN 280
FT /note="F->W: Preserves membrane binding and ability to
FT tubulate liposomes."
FT /evidence="ECO:0000269|PubMed:25284369"
FT MUTAGEN 289
FT /note="T->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 358
FT /note="S->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 389
FT /note="T->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 448
FT /note="R->Q: Loss of GAP activity. No effect on GULP1
FT binding or association with endosomal tubules when
FT coexpressed with PIP5K1C."
FT /evidence="ECO:0000269|PubMed:11062263,
FT ECO:0000269|PubMed:17398097"
FT MUTAGEN 461
FT /note="T->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 554
FT /note="S->A: Loss of phosphorylation by PKB, interaction
FT with ITGB1 and ITGB1-dependent cell migration."
FT /evidence="ECO:0000269|PubMed:16256741,
FT ECO:0000269|PubMed:22645133"
FT MUTAGEN 554
FT /note="S->D: Enhances interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741,
FT ECO:0000269|PubMed:22645133"
FT MUTAGEN 568
FT /note="S->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 711
FT /note="T->A: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 712
FT /note="Y->F: No effect on interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 724
FT /note="S->A: Loss of phosphorylation at S-554, interaction
FT with ITGB1 and ITGB1-dependent cell migration."
FT /evidence="ECO:0000269|PubMed:16256741"
FT MUTAGEN 724
FT /note="S->D: Enhances interaction with ITGB1."
FT /evidence="ECO:0000269|PubMed:16256741"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 15..68
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 74..113
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 118..143
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 149..212
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 214..248
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:4NSW"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:4NSW"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 345..361
FT /evidence="ECO:0007829|PDB:4NSW"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:3JUE"
FT TURN 415..418
FT /evidence="ECO:0007829|PDB:3JUE"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:3JUE"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:3JUE"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:3JUE"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:3JUE"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:3JUE"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:3JUE"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 467..475
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 478..485
FT /evidence="ECO:0007829|PDB:3JUE"
FT TURN 486..493
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 503..514
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 571..578
FT /evidence="ECO:0007829|PDB:3JUE"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 585..593
FT /evidence="ECO:0007829|PDB:3JUE"
FT TURN 603..606
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 610..616
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 620..628
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 643..650
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 653..661
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 676..682
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 686..696
FT /evidence="ECO:0007829|PDB:3JUE"
FT HELIX 713..720
FT /evidence="ECO:0007829|PDB:3T9K"
SQ SEQUENCE 740 AA; 81536 MW; 64891DA3CE00189C CRC64;
MTVKLDFEEC LKDSPRFRAS IELVEAEVSE LETRLEKLLK LGTGLLESGR HYLAASRAFV
VGICDLARLG PPEPMMAECL EKFTVSLNHK LDSHAELLDA TQHTLQQQIQ TLVKEGLRGF
REARRDFWRG AESLEAALTH NAEVPRRRAQ EAEEAGAALR TARAGYRGRA LDYALQINVI
EDKRKFDIME FVLRLVEAQA THFQQGHEEL SRLSQYRKEL GAQLHQLVLN SAREKRDMEQ
RHVLLKQKEL GGEEPEPSLR EGPGGLVMEG HLFKRASNAF KTWSRRWFTI QSNQLVYQKK
YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSTSKSCLL QADSERLLQL WVSAVQSSIA
SAFSQARLDD SPRGPGQGSG HLAIGSAATL GSGGMARGRE PGGVGHVVAQ VQSVDGNAQC
CDCREPAPEW ASINLGVTLC IQCSGIHRSL GVHFSKVRSL TLDSWEPELV KLMCELGNVI
INQIYEARVE AMAVKKPGPS CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGRPRGQP
PVPPKPSIRP RPGSLRSKPE PPSEDLGSLH PGALLFRASG HPPSLPTMAD ALAHGADVNW
VNGGQDNATP LIQATAANSL LACEFLLQNG ANVNQADSAG RGPLHHATIL GHTGLACLFL
KRGADLGARD SEGRDPLTIA METANADIVT LLRLAKMREA EAAQGQAGDE TYLDIFRDFS
LMASDDPEKL SRRSHDLHTL
