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 24-JAN-2024, entry version 206. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-2546; -. DR EMDB; EMD-2547; -. DR SMR; Q15027; -. DR BioGRID; 115092; 16. DR CORUM; Q15027; -. DR IntAct; Q15027; 17. DR MINT; Q15027; -. DR STRING; 9606.ENSP00000158762; -. DR GlyCosmos; Q15027; 2 sites, 2 glycans. 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; 9606-ENSP00000158762; -. DR PeptideAtlas; Q15027; -. DR ProteomicsDB; 60378; -. DR Pumba; Q15027; -. DR Antibodypedia; 24069; 281 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 AGR; HGNC:16467; -. 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; CADHGDI; -. DR OrthoDB; 1449795at2759; -. DR PhylomeDB; Q15027; -. DR TreeFam; TF318315; -. DR PathwayCommons; Q15027; -. DR SignaLink; Q15027; -. DR SIGNOR; Q15027; -. DR BioGRID-ORCS; 9744; 9 hits in 1152 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 94 other cell types or tissues. DR ExpressionAtlas; Q15027; baseline and differential. 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 CDD; cd08852; ArfGap_ACAP1; 1. DR CDD; cd13250; PH_ACAP; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR004148; BAR_dom. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR23180:SF197; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR23180; CENTAURIN/ARF; 1. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF01412; ArfGap; 1. DR Pfam; PF16746; BAR_3; 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; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF50729; PH domain-like; 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. DR Genevisible; Q15027; HS. 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 //