P52907 (CAZA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
F-actin-capping protein subunit alpha-1

Alternative name(s):
CapZ alpha-1

Gene names

Name:

CAPZA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Heterodimer of an alpha and a beta subunit. Interacts with S100A By similarity. 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 S100B. Ref.8
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Sequence similarities	Belongs to the F-actin-capping protein alpha subunit family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
Molecular function	Actin capping
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro actin filament capping Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Traceable author statement. Source: Reactome cellular component movement Traceable author statement PubMed 16130169. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome protein complex assembly Traceable author statement Ref.1. Source: ProtInc
Cellular_component	F-actin capping protein complex Traceable author statement Ref.1. Source: ProtInc WASH complex Inferred from direct assay Ref.8. Source: UniProtKB cytosol Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome
Molecular_function	actin binding Traceable author statement PubMed 7665558. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 286

285

F-actin-capping protein subunit alpha-1

PRO_0000208624

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

19

1

N6-acetyllysine Ref.9

Modified residue

97

1

N6-acetyllysine Ref.9

Experimental info

Sequence conflict

192

1

L → P in BAD96946. Ref.4

Secondary structure

1

.

.

.

286

Helix Strand Turn

Details...

Helix

271 – 275

5

Sequences

	Sequence		Length	Mass (Da)
	P52907 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0F47ADAB6A3689DD	FASTA	286	32,923
	10 20 30 40 50 60 MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD 70 80 90 100 110 120 QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EEADGGLKSW 130 140 150 160 170 180 RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT 190 200 210 220 230 240 ITPPTAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ 250 260 270 280 TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Placenta.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Gastric mucosa.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Cervix.
[7]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12 AND 178-192, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: T-cell.
[8]	"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.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-97, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12." Inman K.G., Yang R., Rustandi R.R., Miller K.E., Baldisseri D.M., Weber D.J. J. Mol. Biol. 324:1003-1014(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM.
[12]	"A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex." McClintock K.A., Shaw G.S. J. Biol. Chem. 278:6251-6257(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U56637 mRNA. Translation: AAC00533.1.
CR407657 mRNA. Translation: CAG28585.1.
CR541819 mRNA. Translation: CAG46618.1.
BT019364 mRNA. Translation: AAV38171.1.
AK223226 mRNA. Translation: BAD96946.1.
AL603832, AL929470 Genomic DNA. Translation: CAI14054.1.
AL929470, AL603832 Genomic DNA. Translation: CAI16528.1.
BC000144 mRNA. Translation: AAH00144.1.

IPI

IPI00005969.

PIR

G02639.

RefSeq

NP_006126.1. NM_006135.2.

UniGene

Hs.514934.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MQ1	NMR	-	C/D	265-276	[»]
1MWN	NMR	-	X/Y	265-276	[»]

ProteinModelPortal

P52907.

ModBase

Search...

Protein-protein interaction databases

IntAct

P52907. 9 interactions.

MINT

MINT-5001076.

STRING

9606.ENSP00000263168.

PTM databases

PhosphoSite

P52907.

Polymorphism databases

DMDM

1705650.

2D gel databases

OGP

P52907.

REPRODUCTION-2DPAGE

IPI00005969.
P52907.

SWISS-2DPAGE

P52907.

Proteomic databases

PaxDb

P52907.

PeptideAtlas

P52907.

PRIDE

P52907.

Protocols and materials databases

DNASU

829.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263168; ENSP00000263168; ENSG00000116489.

GeneID

829.

KEGG

hsa:829.

UCSC

uc001ecj.1. human.

Organism-specific databases

CTD

829.

GeneCards

GC01P113161.

HGNC

HGNC:1488. CAPZA1.

HPA

CAB045963.

MIM

601580. gene.

neXtProt

NX_P52907.

PharmGKB

PA26069.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG261759.

HOGENOM

HOG000036539.

HOVERGEN

HBG050810.

InParanoid

P52907.

KO

K10364.

OMA

MADFDDR.

OrthoDB

EOG45DWQ0.

PhylomeDB

P52907.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

Bgee

P52907.

CleanEx

HS_CAPZA1.

Genevestigator

P52907.

Family and domain databases

InterPro

IPR017865. F-actin_cap_asu_CS.
IPR002189. WASH_F-actin_cap_alpha.
[Graphical view]

PANTHER

PTHR10653. PTHR10653. 1 hit.

Pfam

PF01267. F-actin_cap_A. 1 hit.
[Graphical view]

PRINTS

PR00191. FACTINCAPA.

PROSITE

PS00748. F_ACTIN_CAPPING_A_1. 1 hit.
PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CAPZA1. human.

EvolutionaryTrace

P52907.

GenomeRNAi

829.

NextBio

3414.

SOURCE

Search...

Entry information

Entry name

CAZA1_HUMAN

Accession

Primary (citable) accession number: P52907
Secondary accession number(s): Q53FQ6, Q6FHD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.