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Protein

F-actin-capping protein subunit alpha-2

Gene

CAPZA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

F-actin-capping proteins bind in a Ca2+-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.

GO - Biological processi

  1. barbed-end actin filament capping Source: InterPro
  2. blood coagulation Source: Reactome
  3. innate immune response Source: Reactome
  4. movement of cell or subcellular component Source: ProtInc
  5. protein complex assembly Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25195. Advanced glycosylation endproduct receptor signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit alpha-2
Alternative name(s):
CapZ alpha-2
Gene namesi
Name:CAPZA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:1490. CAPZA2.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: ProtInc
  2. cortical cytoskeleton Source: Ensembl
  3. cytosol Source: Reactome
  4. extracellular region Source: Reactome
  5. extracellular vesicular exosome Source: UniProtKB
  6. F-actin capping protein complex Source: ProtInc
  7. membrane Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26071.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 286285F-actin-capping protein subunit alpha-2PRO_0000208627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP47755.
PaxDbiP47755.
PeptideAtlasiP47755.
PRIDEiP47755.

2D gel databases

DOSAC-COBS-2DPAGEP47755.
OGPiP47755.
REPRODUCTION-2DPAGEP47755.

PTM databases

PhosphoSiteiP47755.

Expressioni

Gene expression databases

BgeeiP47755.
CleanExiHS_CAPZA2.
ExpressionAtlasiP47755. baseline and differential.
GenevestigatoriP47755.

Organism-specific databases

HPAiHPA007470.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 and CCDC53. Interacts with RCSD1/CAPZIP.2 Publications

Protein-protein interaction databases

BioGridi107280. 66 interactions.
IntActiP47755. 14 interactions.
STRINGi9606.ENSP00000354947.

Structurei

3D structure databases

ProteinModelPortaliP47755.
SMRiP47755. Positions 8-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG261759.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiP47755.
KOiK10364.
OMAiRWRSEYV.
PhylomeDBiP47755.
TreeFamiTF314822.

Family and domain databases

InterProiIPR002189. CapZ_alpha.
IPR017865. F-actin_cap_asu_CS.
[Graphical view]
PANTHERiPTHR10653. PTHR10653. 1 hit.
PfamiPF01267. F-actin_cap_A. 1 hit.
[Graphical view]
PRINTSiPR00191. FACTINCAPA.
PROSITEiPS00748. F_ACTIN_CAPPING_A_1. 1 hit.
PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P47755-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA
60 70 80 90 100
AHAFAQYNLD QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH
110 120 130 140 150
LRKEATDPRP CEVENAVESW RTSVETALRA YVKEHYPNGV CTVYGKKIDG
160 170 180 190 200
QQTIIACIES HQFQAKNFWN GRWRSEWKFT ITPSTTQVVG ILKIQVHYYE
210 220 230 240 250
DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ TAISENYQTM
260 270 280
SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
Length:286
Mass (Da):32,949
Last modified:January 23, 2007 - v3
Checksum:iB5E1B617A38E758B
GO
Isoform 2 (identifier: P47755-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-172: VYGKKIDGQQTIIACIESHQFQAKNFWNGR → EWSLEVRMEVYNHSFNHSSGWHLENSGSLL
     173-286: Missing.

Note: No experimental confirmation available.

Show »
Length:172
Mass (Da):19,775
Checksum:iF821EBDB7171C078
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei143 – 17230VYGKK…FWNGR → EWSLEVRMEVYNHSFNHSSG WHLENSGSLL in isoform 2. 1 PublicationVSP_053871Add
BLAST
Alternative sequencei173 – 286114Missing in isoform 2. 1 PublicationVSP_053872Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03269 mRNA. Translation: AAA88848.1.
BT006735 mRNA. Translation: AAP35381.1.
AK294409 mRNA. Translation: BAG57661.1.
AC002543 Genomic DNA. Translation: AAC60382.1.
BC005338 mRNA. Translation: AAH05338.1.
U03851 mRNA. Translation: AAC00534.1.
CCDSiCCDS5768.1. [P47755-1]
PIRiG01229.
RefSeqiNP_006127.1. NM_006136.2. [P47755-1]
UniGeneiHs.446123.

Genome annotation databases

EnsembliENST00000361183; ENSP00000354947; ENSG00000198898. [P47755-1]
GeneIDi830.
KEGGihsa:830.
UCSCiuc003vil.3. human. [P47755-1]

Polymorphism databases

DMDMi1345695.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03269 mRNA. Translation: AAA88848.1.
BT006735 mRNA. Translation: AAP35381.1.
AK294409 mRNA. Translation: BAG57661.1.
AC002543 Genomic DNA. Translation: AAC60382.1.
BC005338 mRNA. Translation: AAH05338.1.
U03851 mRNA. Translation: AAC00534.1.
CCDSiCCDS5768.1. [P47755-1]
PIRiG01229.
RefSeqiNP_006127.1. NM_006136.2. [P47755-1]
UniGeneiHs.446123.

3D structure databases

ProteinModelPortaliP47755.
SMRiP47755. Positions 8-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107280. 66 interactions.
IntActiP47755. 14 interactions.
STRINGi9606.ENSP00000354947.

PTM databases

PhosphoSiteiP47755.

Polymorphism databases

DMDMi1345695.

2D gel databases

DOSAC-COBS-2DPAGEP47755.
OGPiP47755.
REPRODUCTION-2DPAGEP47755.

Proteomic databases

MaxQBiP47755.
PaxDbiP47755.
PeptideAtlasiP47755.
PRIDEiP47755.

Protocols and materials databases

DNASUi830.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361183; ENSP00000354947; ENSG00000198898. [P47755-1]
GeneIDi830.
KEGGihsa:830.
UCSCiuc003vil.3. human. [P47755-1]

Organism-specific databases

CTDi830.
GeneCardsiGC07P116451.
HGNCiHGNC:1490. CAPZA2.
HPAiHPA007470.
MIMi601571. gene.
neXtProtiNX_P47755.
PharmGKBiPA26071.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG261759.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiP47755.
KOiK10364.
OMAiRWRSEYV.
PhylomeDBiP47755.
TreeFamiTF314822.

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25195. Advanced glycosylation endproduct receptor signaling.

Miscellaneous databases

GeneWikiiCAPZA2.
GenomeRNAii830.
NextBioi3418.
PROiP47755.
SOURCEiSearch...

Gene expression databases

BgeeiP47755.
CleanExiHS_CAPZA2.
ExpressionAtlasiP47755. baseline and differential.
GenevestigatoriP47755.

Family and domain databases

InterProiIPR002189. CapZ_alpha.
IPR017865. F-actin_cap_asu_CS.
[Graphical view]
PANTHERiPTHR10653. PTHR10653. 1 hit.
PfamiPF01267. F-actin_cap_A. 1 hit.
[Graphical view]
PRINTSiPR00191. FACTINCAPA.
PROSITEiPS00748. F_ACTIN_CAPPING_A_1. 1 hit.
PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families."
    Barron-Casella E.A., Torres M.A., Scherer S.W., Heng H.H.Q., Tsui L.-C., Casella J.F.
    J. Biol. Chem. 270:21472-21479(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retina.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Amygdala.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  6. "Vertebrates have conserved capping protein alpha isoforms with specific expression patterns."
    Hart M.C., Korshunova Y.O., Cooper J.A.
    Cell Motil. Cytoskeleton 38:120-132(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-286 (ISOFORM 1).
    Tissue: Pancreas.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15.
    Tissue: Platelet.
  8. Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15; 20-66; 122-129 AND 179-210, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma and Mammary carcinoma.
  9. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-86; 147-166 AND 179-226, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ."
    Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C., Cuenda A., Cohen P.
    Biochem. J. 389:127-135(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RCSD1/CAPZIP, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex."
    Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.
    Dev. Cell 17:712-723(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE WASH COMPLEX.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCAZA2_HUMAN
AccessioniPrimary (citable) accession number: P47755
Secondary accession number(s): B4DG50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.