PARVG_MOUSE
ID PARVG_MOUSE Reviewed; 331 AA.
AC Q9ERD8; Q8BH45; Q91X89;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Gamma-parvin;
GN Name=Parvg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, Thymus, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probably plays a role in the regulation of cell adhesion and
CC cytoskeleton organization. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with integrin-linked protein kinase and actin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Constituent of focal adhesions. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in spleen and testis, moderately
CC in lung and weakly in brain and heart. {ECO:0000269|PubMed:11722847}.
CC -!- SIMILARITY: Belongs to the parvin family. {ECO:0000305}.
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DR EMBL; AF312712; AAG29542.1; -; mRNA.
DR EMBL; AK040914; BAC30741.1; -; mRNA.
DR EMBL; AK079881; BAC37772.1; -; mRNA.
DR EMBL; AL626769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011200; AAH11200.1; -; mRNA.
DR CCDS; CCDS27710.1; -.
DR RefSeq; NP_001155972.1; NM_001162500.1.
DR RefSeq; NP_071716.3; NM_022321.4.
DR RefSeq; XP_011244008.1; XM_011245706.2.
DR AlphaFoldDB; Q9ERD8; -.
DR SMR; Q9ERD8; -.
DR BioGRID; 211027; 1.
DR IntAct; Q9ERD8; 1.
DR STRING; 10090.ENSMUSP00000023074; -.
DR iPTMnet; Q9ERD8; -.
DR PhosphoSitePlus; Q9ERD8; -.
DR EPD; Q9ERD8; -.
DR MaxQB; Q9ERD8; -.
DR PaxDb; Q9ERD8; -.
DR PRIDE; Q9ERD8; -.
DR ProteomicsDB; 294161; -.
DR Antibodypedia; 27676; 103 antibodies from 25 providers.
DR DNASU; 64099; -.
DR Ensembl; ENSMUST00000023074; ENSMUSP00000023074; ENSMUSG00000022439.
DR GeneID; 64099; -.
DR KEGG; mmu:64099; -.
DR UCSC; uc007xbz.2; mouse.
DR CTD; 64098; -.
DR MGI; MGI:2158329; Parvg.
DR VEuPathDB; HostDB:ENSMUSG00000022439; -.
DR eggNOG; KOG3631; Eukaryota.
DR GeneTree; ENSGT00950000183194; -.
DR HOGENOM; CLU_047624_0_0_1; -.
DR InParanoid; Q9ERD8; -.
DR OMA; FFIPLCD; -.
DR OrthoDB; 871306at2759; -.
DR TreeFam; TF314025; -.
DR BioGRID-ORCS; 64099; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9ERD8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9ERD8; protein.
DR Bgee; ENSMUSG00000022439; Expressed in granulocyte and 94 other tissues.
DR ExpressionAtlas; Q9ERD8; baseline and differential.
DR Genevisible; Q9ERD8; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
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 SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell adhesion; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Membrane; Reference proteome; Repeat.
FT CHAIN 1..331
FT /note="Gamma-parvin"
FT /id="PRO_0000121586"
FT DOMAIN 44..151
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 210..317
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 18..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBI0"
FT CONFLICT 3
FT /note="L -> S (in Ref. 3; AAH11200)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="N -> S (in Ref. 1; AAG29542)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="K -> T (in Ref. 3; AAH11200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37603 MW; 4EEA891D144444F8 CRC64;
MELEFLYDLL QLPKEVAQPT EEELPRGGKK KYLSPNSKRN PKFEELQKVL MEWINTTLLP
EHIVVRSLEE DMFDGLILHH LFQKLASLKL EVEEISLTSA SQRHKLGVIL EAVNQNLQVE
EKQAKWSVET IFNKDLLATL HLLVALAKRF QPDLPLPDNV QVEVIHIEST KTGLKSDKQV
EQLTECKSHK DQPLQDAFDE LFKLAPEKVH AVQEAIVSFV NQKLERLGLS VQSLDTQFAD
GVILLLLIGQ LEGFFLHLKE FYLTPSSPTE MLHNVTLALD LLKDEGLFSY PVNPEDIVNK
DAKSTLRILY SLFQKHSLRA EGGGAHHATP N
