PARVA_RAT
ID PARVA_RAT Reviewed; 372 AA.
AC Q9HB97;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Alpha-parvin;
DE AltName: Full=Actopaxin;
GN Name=Parva; Synonyms=Actp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ACTIN; PXN AND
RP TGFB1I1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [2]
RP INTERACTION WITH TESK1.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
CC -!- SUBUNIT: Interacts with TGFB1I1 (PubMed:11134073). Interacts with LIMS1
CC (via LD motifs) (By similarity). Interacts with ARHGAP31 (By
CC similarity). Interacts with the actin cytoskeleton (PubMed:11134073).
CC Interacts (via C-terminus) with ILK (By similarity). Interacts (via C-
CC terminus) with TESK1 (via C-terminus); the interaction inhibits TESK1
CC kinase activity (PubMed:15817463). Interacts with PXN/PAXILLIN (via LD
CC motif 4) (PubMed:11134073). {ECO:0000250|UniProtKB:Q9NVD7,
CC ECO:0000269|PubMed:11134073, ECO:0000269|PubMed:15817463}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:11134073}. Cell membrane
CC {ECO:0000269|PubMed:11134073}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11134073}; Cytoplasmic side
CC {ECO:0000269|PubMed:11134073}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11134073}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250}. Note=Constituent of focal adhesions.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11134073}.
CC -!- SIMILARITY: Belongs to the parvin family. {ECO:0000305}.
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DR EMBL; AF264765; AAG09802.2; -; mRNA.
DR RefSeq; NP_065707.2; NM_020656.2.
DR AlphaFoldDB; Q9HB97; -.
DR BMRB; Q9HB97; -.
DR SMR; Q9HB97; -.
DR BioGRID; 248617; 1.
DR IntAct; Q9HB97; 4.
DR STRING; 10116.ENSRNOP00000021671; -.
DR iPTMnet; Q9HB97; -.
DR PhosphoSitePlus; Q9HB97; -.
DR jPOST; Q9HB97; -.
DR PaxDb; Q9HB97; -.
DR PRIDE; Q9HB97; -.
DR GeneID; 57341; -.
DR KEGG; rno:57341; -.
DR UCSC; RGD:71021; rat.
DR CTD; 55742; -.
DR RGD; 71021; Parva.
DR eggNOG; KOG3631; Eukaryota.
DR InParanoid; Q9HB97; -.
DR OrthoDB; 871306at2759; -.
DR PhylomeDB; Q9HB97; -.
DR Reactome; R-RNO-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-RNO-446353; Cell-extracellular matrix interactions.
DR Reactome; R-RNO-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR PRO; PR:Q9HB97; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IC:RGD.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:RGD.
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:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS: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: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; ISS: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 Acetylation; Actin-binding; Angiogenesis; Cell adhesion; Cell junction;
KW Cell membrane; Cell shape; Chemotaxis; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; 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_0000121582"
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..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..25
FT /note="Interaction with ARHGAP31"
FT /evidence="ECO:0000250|UniProtKB:Q9EPC1"
FT REGION 223..372
FT /note="Required for interaction with TESK1 and ILK"
FT /evidence="ECO:0000250|UniProtKB:Q9NVD7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPC1"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVD7"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVD7"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVD7"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVD7"
SQ SEQUENCE 372 AA; 42292 MW; 7AAD24EBC25D094C CRC64;
MATSPQKSPS VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSEFQ EEGMNAINLP
LSPISFELDP EDTMLEENEV RTMVDPNSRN DPKLQELMKV LIDWINDVLV GERIIVKDLA
EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE IAQKQKLQTV LEKINEALKL PPRSIKWNVD
SVHAKNLVAI LHLLVALSQY FRAPIRLPDH VSIQVVVVQK REGILQSRQI QEEITGNTEA
LSGRHERDAF DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVTELETQF ADGVYLVLLM
GLLEGYFVPL HSFFLTPDSF EQKVLNVSFA FELMQDGGLE KPKPRPEDIV NCDLKSTLRV
LYNLFTKYRN VE
