CAZA3_HUMAN
ID CAZA3_HUMAN Reviewed; 299 AA.
AC Q96KX2; Q969J0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=F-actin-capping protein subunit alpha-3;
DE AltName: Full=CapZ alpha-3;
DE Short=CP-alpha-3;
DE AltName: Full=Germ cell-specific protein 3;
GN Name=CAPZA3; Synonyms=CAPAA3, GSG3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12029070; DOI=10.1093/molehr/8.6.531;
RA Miyagawa Y., Tanaka H., Iguchi N., Kitamura K., Nakamura Y., Takahashi T.,
RA Matsumiya K., Okuyama A., Nishimune Y.;
RT "Molecular cloning and characterization of the human orthologue of male
RT germ cell-specific actin capping protein alpha3 (cpalpha3).";
RL Mol. Hum. Reprod. 8:531-539(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP IDENTIFICATION IN THE WASH COMPLEX.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC to the fast growing ends of actin filaments (barbed end) thereby
CC blocking the exchange of subunits at these ends. Unlike other capping
CC proteins (such as gelsolin and severin), these proteins do not sever
CC actin filaments. May play a role in the morphogenesis of spermatid (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By similarity).
CC Component of the WASH complex, composed of F-actin-capping protein
CC subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein
CC subunit beta (CAPZB), WASH (WASHC1, WASH2P, WASH3P, WASH4P, WASH5P or
CC WASH6P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5.
CC {ECO:0000250, ECO:0000269|PubMed:19922875}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in testis and sperm. Highest
CC expression is found in the neck region of ejaculated sperm with lower
CC levels found in the tail and postacrosome region.
CC {ECO:0000269|PubMed:12029070}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; AB053259; BAB61901.1; -; mRNA.
DR EMBL; AK058174; BAB71703.1; -; mRNA.
DR EMBL; BC016745; AAH16745.1; -; mRNA.
DR CCDS; CCDS8681.1; -.
DR RefSeq; NP_201585.1; NM_033328.2.
DR AlphaFoldDB; Q96KX2; -.
DR SMR; Q96KX2; -.
DR BioGRID; 125049; 1.
DR CORUM; Q96KX2; -.
DR STRING; 9606.ENSP00000326238; -.
DR GlyConnect; 2866; 1 O-Linked glycan (1 site).
DR GlyGen; Q96KX2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96KX2; -.
DR PhosphoSitePlus; Q96KX2; -.
DR BioMuta; CAPZA3; -.
DR DMDM; 20137887; -.
DR MassIVE; Q96KX2; -.
DR PaxDb; Q96KX2; -.
DR PeptideAtlas; Q96KX2; -.
DR PRIDE; Q96KX2; -.
DR ProteomicsDB; 77129; -.
DR Antibodypedia; 23887; 100 antibodies from 23 providers.
DR DNASU; 93661; -.
DR Ensembl; ENST00000317658.5; ENSP00000326238.3; ENSG00000177938.5.
DR GeneID; 93661; -.
DR KEGG; hsa:93661; -.
DR MANE-Select; ENST00000317658.5; ENSP00000326238.3; NM_033328.3; NP_201585.1.
DR UCSC; uc001rdy.4; human.
DR CTD; 93661; -.
DR GeneCards; CAPZA3; -.
DR HGNC; HGNC:24205; CAPZA3.
DR HPA; ENSG00000177938; Tissue enriched (testis).
DR MIM; 608722; gene.
DR neXtProt; NX_Q96KX2; -.
DR OpenTargets; ENSG00000177938; -.
DR PharmGKB; PA134990260; -.
DR VEuPathDB; HostDB:ENSG00000177938; -.
DR eggNOG; KOG0836; Eukaryota.
DR GeneTree; ENSGT00950000183119; -.
DR HOGENOM; CLU_045161_0_0_1; -.
DR InParanoid; Q96KX2; -.
DR OMA; VMGDFRF; -.
DR OrthoDB; 1085166at2759; -.
DR PhylomeDB; Q96KX2; -.
DR TreeFam; TF314822; -.
DR PathwayCommons; Q96KX2; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR SignaLink; Q96KX2; -.
DR BioGRID-ORCS; 93661; 11 hits in 1070 CRISPR screens.
DR GenomeRNAi; 93661; -.
DR Pharos; Q96KX2; Tdark.
DR PRO; PR:Q96KX2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96KX2; protein.
DR Bgee; ENSG00000177938; Expressed in left testis and 47 other tissues.
DR ExpressionAtlas; Q96KX2; baseline.
DR Genevisible; Q96KX2; HS.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR Gene3D; 3.30.1140.60; -; 1.
DR Gene3D; 3.90.1150.210; -; 1.
DR InterPro; IPR002189; CapZ_alpha.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR042489; CapZ_alpha_1.
DR InterPro; IPR017865; F-actin_cap_asu_CS.
DR PANTHER; PTHR10653; PTHR10653; 1.
DR Pfam; PF01267; F-actin_cap_A; 1.
DR PRINTS; PR00191; FACTINCAPA.
DR SUPFAM; SSF90096; SSF90096; 1.
DR PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..299
FT /note="F-actin-capping protein subunit alpha-3"
FT /id="PRO_0000208631"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUV6"
FT CONFLICT 95
FT /note="D -> Y (in Ref. 3; AAH16745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 35025 MW; CEE130C8F7397F67 CRC64;
MTLSVLSRKD KERVIRRLLL QAPPGEFVNA FDDLCLLIRD EKLMHHQGEC AGHQHCQKYS
VPLCIDGNPV LLSHHNVMGD YRFFDHQSKL SFKYDLLQNQ LKDIQSHGII QNEAEYLRVV
LLCALKLYVN DHYPKGNCNM LRKTVKSKEY LIACIEDHNY ETGECWNGLW KSKWIFQVNP
FLTQVTGRIF VQAHFFRCVN LHIEISKDLK ESLEIVNQAQ LALSFARLVE EQENKFQAAV
LEELQELSNE ALRKILRRDL PVTRTLIDWH RILSDLNLVM YPKLGYVIYS RSVLCNWII
