CAZA3_MOUSE
ID CAZA3_MOUSE Reviewed; 299 AA.
AC P70190; Q9D4N3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=F-actin-capping protein subunit alpha-3;
DE AltName: Full=CapZ alpha-3;
DE AltName: Full=Germ cell-specific protein 3;
GN Name=Capza3; Synonyms=Cappa3, Gsg3;
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].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=7957958; DOI=10.1016/0014-5793(94)01155-9;
RA Tanaka H., Yoshimura Y., Nishina Y., Nozaki M., Nojima H., Nishimune Y.;
RT "Isolation and characterization of cDNA clones specifically expressed in
RT testicular germ cells.";
RL FEBS Lett. 355:4-10(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10524250; DOI=10.1016/s0378-1119(99)00287-5;
RA Yoshimura Y., Tanaka H., Nozaki M., Yomogida K., Shimamura K., Yasunaga T.,
RA Nishimune Y.;
RT "Genomic analysis of male germ cell-specific actin capping protein alpha.";
RL Gene 237:193-199(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
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).
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.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the
CC WASH complex, composed of F-actin-capping protein subunit alpha
CC (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta
CC (CAPZB), WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5 (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in the testis.
CC -!- DEVELOPMENTAL STAGE: Expressed in 24-day-old and adult testis, but not
CC in 4-, 10- and 16-day-old testis.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; D87471; BAA13409.1; -; mRNA.
DR EMBL; AB026984; BAA81887.1; -; Genomic_DNA.
DR EMBL; AK016391; BAB30213.1; -; mRNA.
DR EMBL; BC049620; AAH49620.1; -; mRNA.
DR CCDS; CCDS20672.1; -.
DR RefSeq; NP_031631.3; NM_007605.4.
DR AlphaFoldDB; P70190; -.
DR SMR; P70190; -.
DR STRING; 10090.ENSMUSP00000038562; -.
DR PhosphoSitePlus; P70190; -.
DR PaxDb; P70190; -.
DR PRIDE; P70190; -.
DR ProteomicsDB; 265677; -.
DR Antibodypedia; 23887; 100 antibodies from 23 providers.
DR DNASU; 12344; -.
DR Ensembl; ENSMUST00000043797; ENSMUSP00000038562; ENSMUSG00000041791.
DR GeneID; 12344; -.
DR KEGG; mmu:12344; -.
DR UCSC; uc009eoa.2; mouse.
DR CTD; 93661; -.
DR MGI; MGI:106221; Capza3.
DR VEuPathDB; HostDB:ENSMUSG00000041791; -.
DR eggNOG; KOG0836; Eukaryota.
DR GeneTree; ENSGT00950000183119; -.
DR HOGENOM; CLU_045161_0_0_1; -.
DR InParanoid; P70190; -.
DR OMA; VMGDFRF; -.
DR OrthoDB; 1085166at2759; -.
DR PhylomeDB; P70190; -.
DR TreeFam; TF314822; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 12344; 1 hit in 72 CRISPR screens.
DR PRO; PR:P70190; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P70190; protein.
DR Bgee; ENSMUSG00000041791; Expressed in seminiferous tubule of testis and 5 other tissues.
DR Genevisible; P70190; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
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 2: Evidence at transcript 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_0000208632"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUV6"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUV6"
FT CONFLICT 117
FT /note="L -> I (in Ref. 3; BAB30213)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="F -> Y (in Ref. 3; BAB30213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 34952 MW; 8C87579313F233C6 CRC64;
MSLSVLSRKE KEKVIHRLLV QAPPGEFVNA FDDLCLLIRD EKLMHHQGEC AGHQHCQKYC
VPLCIDGNPV LLSHHNVMGD FRFFDYQSKL SFRFDLLQNQ LRDIQSHGII RNETEYLRSV
VMCALKLYVN DHYPNGNCNV LRKTVKSKEF LIACIEDHSY DNGECWNGLW KSKWIFQVNP
FLTQVTGRIF VQAHFFRCVN LHIEVSKDLK ESLEVVNQAQ LALSFARLVE EQENKFQAAV
IEELQELSNE ALRKILRRDL PVTRTLIDWQ RILSDLNLVM YPKLGYVIYS RSVLCNWII
