Reviewed, UniProtKB/Swiss-Prot Q9NVD7 (PARVA_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-parvin
Alternative name(s):
    Calponin-like integrin-linked kinase-binding protein
    CH-ILKBP
    Matrix-remodeling-associated protein 2
    Actopaxin

Gene names

Name:	PARVA
Synonyms:	MXRA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Ref.6
Subunit structure	Interacts with TGFB1I1 By similarity. Interacts with integrin-linked protein kinase and probably with actin and the LD1 and LD4 motifs of PXN. Interacts with CDGAP. Ref.8
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Note: Constituent of focal adhesions. Ref.6
Tissue specificity	Widely expressed, with highest levels in heart, skeletal muscle, kidney and liver. Ref.6 Ref.7
Sequence similarities	Belongs to the parvin family. Contains 2 CH (calponin-homology) domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from Experiment. Source: Reactome extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DHX36	Q9H2U1	1	EBI-747655,EBI-1047643

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NVD7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NVD7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     134-182: EKLESEKLNV...RSIKWNVDSV → GRRVECCNGC...KCVEHGITAQ
     183-372: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 372

372

Alpha-parvin

PRO_0000121580

Regions

Domain

95 – 201

107

CH 1

Domain

262 – 369

108

CH 2

Region

21 – 25

5

Interaction with CDGAP

Amino acid modifications

Modified residue

4

1

Phosphoserine Ref.9

Modified residue

8

1

Phosphoserine Ref.9

Modified residue

14

1

Phosphoserine Ref.10

Modified residue

19

1

Phosphoserine Ref.10

Modified residue

28

1

Phosphoserine Ref.9

Modified residue

36

1

Phosphothreonine Ref.9 Ref.10

Modified residue

62

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

134 – 182

49

EKLES…NVDSV → GRRVECCNGCVFNCRWLDHL LVARRSYSQFTVAYLEMDYK CVEHGITAQ in isoform 2.

VSP_008884

Alternative sequence

183 – 372

190

Missing in isoform 2.

VSP_008885

Experimental info

Sequence conflict

11

1

V → A in AAH14535. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

372

Helix Strand Turn

Details...

Helix

249 – 256

8

Helix

258 – 279

22

Helix

286 – 289

4

Beta strand

290 – 293

4

Helix

294 – 304

11

Beta strand

312 – 314

3

Helix

320 – 337

18

Helix

346 – 350

5

Helix

355 – 368

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F48BB5B1E83F8CEF	FASTA	372	42,244
	10 20 30 40 50 60 MATSPQKSPS VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSELQ EEGMNAINLP 70 80 90 100 110 120 LSPIPFELDP EDTMLEENEV RTMVDPNSRS DPKLQELMKV LIDWINDVLV GERIIVKDLA 130 140 150 160 170 180 EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE IAQKQKLQTV LEKINETLKL PPRSIKWNVD 190 200 210 220 230 240 SVHAKSLVAI LHLLVALSQY FRAPIRLPDH VSIQVVVVQK REGILQSRQI QEEITGNTEA 250 260 270 280 290 300 LSGRHERDAF DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVTELETQF ADGVYLVLLM 310 320 330 340 350 360 GLLEGYFVPL HSFFLTPDSF EQKVLNVSFA FELMQDGGLE KPKPRPEDIV NCDLKSTLRV 370 LYNLFTKYRN VE
	Isoform 2. Checksum: B7D6685D209E628F	FASTA	182	20,625
	10 20 30 40 50 60 MATSPQKSPS VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSELQ EEGMNAINLP 70 80 90 100 110 120 LSPIPFELDP EDTMLEENEV RTMVDPNSRS DPKLQELMKV LIDWINDVLV GERIIVKDLA 130 140 150 160 170 180 EDLYDGQVLQ KLFGRRVECC NGCVFNCRWL DHLLVARRSY SQFTVAYLEM DYKCVEHGIT AQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily." Olski T.M., Noegel A.A., Korenbaum E. J. Cell Sci. 114:525-538(2001) [PubMed: 11171322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading." Tu Y., Huang Y., Zhang Y., Hua Y., Wu C. J. Cell Biol. 153:585-598(2001) [PubMed: 11331308] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Mammary gland.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed: 15242332] [Abstract] Cited for: PROTEIN SEQUENCE OF 118-131. Tissue: Adipocyte.
[6]	"Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion." Nikolopoulos S.N., Turner C.E. J. Cell Biol. 151:1435-1448(2000) [PubMed: 11134073] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]	"Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans." Korenbaum E., Olski T.M., Noegel A.A. Gene 279:69-79(2001) [PubMed: 11722847] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"CdGAP associates with actopaxin to regulate integrin-dependent changes in cell morphology and motility." LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E. Curr. Biol. 16:1375-1385(2006) [PubMed: 16860736] [Abstract] Cited for: INTERACTION WITH CDGAP.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-8; SER-28; THR-36 AND SER-62, MASS SPECTROMETRY.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-19 AND THR-36, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF237771 mRNA. Translation: AAG27173.1.
AF325830 mRNA. Translation: AAK49911.1.
AK001655 mRNA. Translation: BAA91815.1.
AK022316 mRNA. Translation: BAB14009.1.
BC016713 mRNA. Translation: AAH16713.1.
BC014535 mRNA. Translation: AAH14535.1.

IPI

IPI00018963.
IPI00386908.

RefSeq

NP_060692.1.

UniGene

Hs.607144

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K2R	NMR	-	A	244-372	[»]
2VZC	X-ray	1.05	A/B	242-372	[»]
2VZD	X-ray	2.10	A/B	242-372	[»]
2VZG	X-ray	1.80	B	242-372	[»]
2VZI	X-ray	2.20	B	242-372	[»]
3KMU	X-ray	1.80	B	248-372	[»]
3KMW	X-ray	2.00	B	248-372	[»]

SMR

Q9NVD7. Positions 98-365.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46239N.

IntAct

Q9NVD7. 3 interactions.

STRING

Q9NVD7.

PTM databases

PhosphoSite

Q9NVD7.

Proteomic databases

PRIDE

Q9NVD7.

Genome annotation databases

Ensembl

ENST00000334956; ENSP00000334008; ENSG00000197702; Homo sapiens. [Genome view]

GeneID

55742.

KEGG

hsa:55742.

UCSC

uc001mkh.2. human.
uc001mki.2. human.

Organism-specific databases

CTD

55742.

GeneCards

GC11P012355.

H-InvDB

HIX0009455.

HGNC

HGNC:14652. PARVA.

HPA

HPA005964.

MIM

608120. gene.

PharmGKB

PA32950.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13695.

HOGENOM

HBG447386.

HOVERGEN

Q9NVD7.

InParanoid

Q9NVD7.

OMA

NTEYVNT.

OrthoDB

EOG9RZ1JR.

Enzyme and pathway databases

Reactome

REACT_20676. Cell junction organization.

Gene expression databases

ArrayExpress

Q9NVD7.

Bgee

Q9NVD7.

CleanEx

HS_PARVA.

Genevestigator

Q9NVD7.

GermOnline

ENSG00000197702. Homo sapiens.

Family and domain databases

InterPro

IPR016146. Calponin-homology.
IPR001715. Calponin_act_bd.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 2 hits.

Pfam

PF00307. CH. 2 hits.
[Graphical view]

SMART

SM00033. CH. 2 hits.
[Graphical view]

PROSITE

PS50021. CH. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

60703.

SOURCE

Search...

Entry information

Entry name

PARVA_HUMAN

Accession

Primary (citable) accession number: Q9NVD7
Secondary accession number(s): Q96C85, Q9HA48

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.