PARVA_HUMAN
ID PARVA_HUMAN Reviewed; 372 AA.
AC Q9NVD7; Q96C85; Q9HA48;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Alpha-parvin;
DE AltName: Full=Actopaxin;
DE AltName: Full=CH-ILKBP;
DE AltName: Full=Calponin-like integrin-linked kinase-binding protein;
DE AltName: Full=Matrix-remodeling-associated protein 2;
GN Name=PARVA; Synonyms=MXRA2;
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).
RX PubMed=11171322; DOI=10.1242/jcs.114.3.525;
RA Olski T.M., Noegel A.A., Korenbaum E.;
RT "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin
RT superfamily.";
RL J. Cell Sci. 114:525-538(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ILK;
RP LIMS1 AND WITH ACTIN CYTOSKELETON, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11331308; DOI=10.1083/jcb.153.3.585;
RA Tu Y., Huang Y., Zhang Y., Hua Y., Wu C.;
RT "A new focal adhesion protein that interacts with integrin-linked kinase
RT and regulates cell adhesion and spreading.";
RL J. Cell Biol. 153:585-598(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 118-131.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11134073; DOI=10.1083/jcb.151.7.1435;
RA Nikolopoulos S.N., Turner C.E.;
RT "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and
RT actin and regulates cell adhesion.";
RL J. Cell Biol. 151:1435-1448(2000).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11722847; DOI=10.1016/s0378-1119(01)00743-0;
RA Korenbaum E., Olski T.M., Noegel A.A.;
RT "Genomic organization and expression profile of the parvin family of focal
RT adhesion proteins in mice and humans.";
RL Gene 279:69-79(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH ILK.
RX PubMed=15284246; DOI=10.1074/jbc.m401563200;
RA Zhang Y., Chen K., Tu Y., Wu C.;
RT "Distinct roles of two structurally closely related focal adhesion
RT proteins, alpha-parvins and beta-parvins, in regulation of cell morphology
RT and survival.";
RL J. Biol. Chem. 279:41695-41705(2004).
RN [9]
RP INTERACTION WITH ILK; PXN AND TESK1, AND MUTAGENESIS OF SER-4 AND SER-8.
RX PubMed=15817463; DOI=10.1074/jbc.m500752200;
RA LaLonde D.P., Brown M.C., Bouverat B.P., Turner C.E.;
RT "Actopaxin interacts with TESK1 to regulate cell spreading on
RT fibronectin.";
RL J. Biol. Chem. 280:21680-21688(2005).
RN [10]
RP INTERACTION WITH ARHGAP31.
RX PubMed=16860736; DOI=10.1016/j.cub.2006.05.057;
RA LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E.;
RT "CdGAP associates with actopaxin to regulate integrin-dependent changes in
RT cell morphology and motility.";
RL Curr. Biol. 16:1375-1385(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-19, AND
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 [13]
RP FUNCTION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T.,
RA Aza-Blanc P., Gleeson J.G.;
RT "Functional genomic screen for modulators of ciliogenesis and cilium
RT length.";
RL Nature 464:1048-1051(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=22441983; DOI=10.1096/fj.11-193383;
RA Devalliere J., Chatelais M., Fitau J., Gerard N., Hulin P., Velazquez L.,
RA Turner C.E., Charreau B.;
RT "LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells
RT and targets alpha-parvin to control cell adhesion and migration.";
RL FASEB J. 26:2592-2606(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-14 AND SER-19, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-19, AND
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 [19]
RP STRUCTURE BY NMR OF 244-372 IN COMPLEX WITH PXN, AND INTERACTION WITH PXN.
RX PubMed=18508764; DOI=10.1074/jbc.m801270200;
RA Wang X., Fukuda K., Byeon I.J., Velyvis A., Wu C., Gronenborn A., Qin J.;
RT "The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel
RT modular recognition for focal adhesion assembly.";
RL J. Biol. Chem. 283:21113-21119(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 242-372 IN COMPLEX WITH PXN, AND
RP INTERACTION WITH PXN.
RX PubMed=18940607; DOI=10.1016/j.str.2008.08.007;
RA Lorenz S., Vakonakis I., Lowe E.D., Campbell I.D., Noble M.E.,
RA Hoellerer M.K.;
RT "Structural analysis of the interactions between paxillin LD motifs and
RT alpha-parvin.";
RL Structure 16:1521-1531(2008).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 248-372 IN COMPLEX WITH ILK, AND
RP INTERACTION WITH ILK.
RX PubMed=20005845; DOI=10.1016/j.molcel.2009.11.028;
RA Fukuda K., Gupta S., Chen K., Wu C., Qin J.;
RT "The pseudoactive site of ILK is essential for its binding to alpha-parvin
RT and localization to focal adhesions.";
RL Mol. Cell 36:819-830(2009).
CC -!- FUNCTION: Plays a role in sarcomere organization and in smooth muscle
CC cell contraction. Required for normal development of the embryonic
CC cardiovascular system, and for normal septation of the heart outflow
CC tract. Plays a role in sprouting angiogenesis and is required for
CC normal adhesion of vascular smooth muscle cells to endothelial cells
CC during blood vessel development (By similarity). Plays a role in the
CC reorganization of the actin cytoskeleton, formation of lamellipodia and
CC ciliogenesis. Plays a role in the establishment of cell polarity, cell
CC adhesion, cell spreading, and directed cell migration. {ECO:0000250,
CC ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:11331308,
CC ECO:0000269|PubMed:15284246, ECO:0000269|PubMed:20393563}.
CC -!- SUBUNIT: Interacts with TGFB1I1 (By similarity). Interacts with LIMS1
CC (via LD motifs) (PubMed:11331308). Interacts with ARHGAP31
CC (PubMed:16860736). Interacts with the actin cytoskeleton
CC (PubMed:11331308). Interacts (via C-terminus) with ILK
CC (PubMed:11331308, PubMed:15284246, PubMed:15817463, PubMed:20005845).
CC Interacts (via C-terminus) with TESK1 (via C-terminus); the interaction
CC inhibits TESK1 kinase activity (PubMed:15817463). Interacts with
CC PXN/PAXILLIN (via LD motif 4) (PubMed:15817463, PubMed:18508764,
CC PubMed:18940607). {ECO:0000250, ECO:0000250|UniProtKB:Q9EPC1,
CC ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:15284246,
CC ECO:0000269|PubMed:15817463, ECO:0000269|PubMed:16860736,
CC ECO:0000269|PubMed:18508764, ECO:0000269|PubMed:18940607,
CC ECO:0000269|PubMed:20005845}.
CC -!- INTERACTION:
CC Q9NVD7; P54252: ATXN3; NbExp=9; IntAct=EBI-747655, EBI-946046;
CC Q9NVD7; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-747655, EBI-744099;
CC Q9NVD7; Q13418: ILK; NbExp=23; IntAct=EBI-747655, EBI-747644;
CC Q9NVD7; Q96EN8: MOCOS; NbExp=5; IntAct=EBI-747655, EBI-1220583;
CC Q9NVD7; O55222: Ilk; Xeno; NbExp=2; IntAct=EBI-747655, EBI-6690138;
CC Q9NVD7-1; P49023-2: PXN; NbExp=3; IntAct=EBI-15735104, EBI-11954250;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
CC Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Constituent
CC of focal adhesions. Associates with the actin cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NVD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVD7-2; Sequence=VSP_008884, VSP_008885;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart,
CC skeletal muscle, kidney and liver. {ECO:0000269|PubMed:11134073,
CC ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:11722847}.
CC -!- SIMILARITY: Belongs to the parvin family. {ECO:0000305}.
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DR EMBL; AF237771; AAG27173.1; -; mRNA.
DR EMBL; AF325830; AAK49911.1; -; mRNA.
DR EMBL; AK001655; BAA91815.1; -; mRNA.
DR EMBL; AK022316; BAB14009.1; -; mRNA.
DR EMBL; BC016713; AAH16713.1; -; mRNA.
DR EMBL; BC014535; AAH14535.1; -; mRNA.
DR CCDS; CCDS44541.2; -. [Q9NVD7-1]
DR RefSeq; NP_060692.2; NM_018222.4. [Q9NVD7-1]
DR PDB; 2K2R; NMR; -; A=244-372.
DR PDB; 2VZC; X-ray; 1.05 A; A/B=242-372.
DR PDB; 2VZD; X-ray; 2.10 A; A/B=242-372.
DR PDB; 2VZG; X-ray; 1.80 A; B=242-372.
DR PDB; 2VZI; X-ray; 2.20 A; B=242-372.
DR PDB; 3KMU; X-ray; 1.80 A; B=248-372.
DR PDB; 3KMW; X-ray; 2.00 A; B=248-372.
DR PDB; 3REP; X-ray; 1.80 A; B=248-372.
DR PDB; 6MIB; X-ray; 1.80 A; B=248-372.
DR PDBsum; 2K2R; -.
DR PDBsum; 2VZC; -.
DR PDBsum; 2VZD; -.
DR PDBsum; 2VZG; -.
DR PDBsum; 2VZI; -.
DR PDBsum; 3KMU; -.
DR PDBsum; 3KMW; -.
DR PDBsum; 3REP; -.
DR PDBsum; 6MIB; -.
DR AlphaFoldDB; Q9NVD7; -.
DR BMRB; Q9NVD7; -.
DR SMR; Q9NVD7; -.
DR BioGRID; 120860; 73.
DR CORUM; Q9NVD7; -.
DR IntAct; Q9NVD7; 32.
DR MINT; Q9NVD7; -.
DR STRING; 9606.ENSP00000334008; -.
DR iPTMnet; Q9NVD7; -.
DR PhosphoSitePlus; Q9NVD7; -.
DR BioMuta; PARVA; -.
DR DMDM; 20139236; -.
DR EPD; Q9NVD7; -.
DR jPOST; Q9NVD7; -.
DR MassIVE; Q9NVD7; -.
DR MaxQB; Q9NVD7; -.
DR PaxDb; Q9NVD7; -.
DR PeptideAtlas; Q9NVD7; -.
DR PRIDE; Q9NVD7; -.
DR ProteomicsDB; 82782; -. [Q9NVD7-1]
DR ProteomicsDB; 82783; -. [Q9NVD7-2]
DR Antibodypedia; 993; 458 antibodies from 32 providers.
DR DNASU; 55742; -.
DR Ensembl; ENST00000334956.15; ENSP00000334008.9; ENSG00000197702.14. [Q9NVD7-1]
DR GeneID; 55742; -.
DR KEGG; hsa:55742; -.
DR MANE-Select; ENST00000334956.15; ENSP00000334008.9; NM_018222.5; NP_060692.3.
DR CTD; 55742; -.
DR DisGeNET; 55742; -.
DR GeneCards; PARVA; -.
DR HGNC; HGNC:14652; PARVA.
DR HPA; ENSG00000197702; Low tissue specificity.
DR MIM; 608120; gene.
DR neXtProt; NX_Q9NVD7; -.
DR OpenTargets; ENSG00000197702; -.
DR PharmGKB; PA32950; -.
DR VEuPathDB; HostDB:ENSG00000197702; -.
DR eggNOG; KOG3631; Eukaryota.
DR GeneTree; ENSGT00950000183194; -.
DR InParanoid; Q9NVD7; -.
DR OMA; QIRIEVP; -.
DR OrthoDB; 871306at2759; -.
DR PhylomeDB; Q9NVD7; -.
DR PathwayCommons; Q9NVD7; -.
DR Reactome; R-HSA-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
DR Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR SignaLink; Q9NVD7; -.
DR SIGNOR; Q9NVD7; -.
DR BioGRID-ORCS; 55742; 35 hits in 1068 CRISPR screens.
DR ChiTaRS; PARVA; human.
DR EvolutionaryTrace; Q9NVD7; -.
DR GeneWiki; PARVA; -.
DR GenomeRNAi; 55742; -.
DR Pharos; Q9NVD7; Tbio.
DR PRO; PR:Q9NVD7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NVD7; protein.
DR Bgee; ENSG00000197702; Expressed in smooth muscle tissue and 208 other tissues.
DR ExpressionAtlas; Q9NVD7; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0070252; P:actin-mediated cell contraction; ISS:UniProtKB.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; TAS:ARUK-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0071670; P:smooth muscle cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR028433; Parvin.
DR PANTHER; PTHR12114; PTHR12114; 1.
DR Pfam; PF00307; CH; 2.
DR PIRSF; PIRSF039131; Parvin; 1.
DR SMART; SM00033; CH; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Angiogenesis; Cell adhesion; Cell junction; Cell membrane; Cell shape;
KW Chemotaxis; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9EPC1"
FT CHAIN 2..372
FT /note="Alpha-parvin"
FT /id="PRO_0000121580"
FT DOMAIN 95..202
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 262..369
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..25
FT /note="Interaction with ARHGAP31"
FT /evidence="ECO:0000269|PubMed:16860736"
FT REGION 223..372
FT /note="Required for interaction with TESK1 and ILK"
FT /evidence="ECO:0000269|PubMed:15817463"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPC1"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 134..182
FT /note="EKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSV ->
FT GRRVECCNGCVFNCRWLDHLLVARRSYSQFTVAYLEMDYKCVEHGITAQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008884"
FT VAR_SEQ 183..372
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008885"
FT MUTAGEN 4
FT /note="S->D: Loss of interaction with TESK1, however no
FT effect on interaction with ILK; when associated with D-8."
FT /evidence="ECO:0000269|PubMed:15817463"
FT MUTAGEN 8
FT /note="S->D: Loss of interaction with TESK1, however no
FT effect on interaction with ILK; when associated with D-4."
FT /evidence="ECO:0000269|PubMed:15817463"
FT CONFLICT 11
FT /note="V -> A (in Ref. 4; AAH14535)"
FT /evidence="ECO:0000305"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:2VZC"
FT HELIX 258..276
FT /evidence="ECO:0007829|PDB:2VZC"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2VZC"
FT TURN 286..292
FT /evidence="ECO:0007829|PDB:2VZC"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:2VZC"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:2VZG"
FT HELIX 320..336
FT /evidence="ECO:0007829|PDB:2VZC"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:2VZC"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:2VZC"
SQ SEQUENCE 372 AA; 42244 MW; F48BB5B1E83F8CEF CRC64;
MATSPQKSPS VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSELQ EEGMNAINLP
LSPIPFELDP EDTMLEENEV RTMVDPNSRS DPKLQELMKV LIDWINDVLV GERIIVKDLA
EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE IAQKQKLQTV LEKINETLKL PPRSIKWNVD
SVHAKSLVAI LHLLVALSQY FRAPIRLPDH VSIQVVVVQK REGILQSRQI QEEITGNTEA
LSGRHERDAF DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVTELETQF ADGVYLVLLM
GLLEGYFVPL HSFFLTPDSF EQKVLNVSFA FELMQDGGLE KPKPRPEDIV NCDLKSTLRV
LYNLFTKYRN VE
