ACTZ_MOUSE
ID ACTZ_MOUSE Reviewed; 376 AA.
AC P61164; P42024; Q3TJF9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Alpha-centractin;
DE Short=Centractin;
DE AltName: Full=ARP1;
DE AltName: Full=Actin-RPV;
DE AltName: Full=Centrosome-associated actin homolog;
GN Name=Actr1a; Synonyms=Ctrn1;
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 TISSUE=Diaphragm;
RX PubMed=9200982; DOI=10.2108/zsj.14.77;
RA Kusano K., Abe H., Obinata T.;
RT "Primary structure of mouse actin-related protein 1 (Arp1) and its tissue
RT expression.";
RL Zool. Sci. 14:77-82(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Placenta, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of a multi-subunit complex involved in microtubule
CC based vesicle motility. It is associated with the centrosome.
CC -!- SUBUNIT: Interacts with BCCIP. {ECO:0000250|UniProtKB:P61163}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P85515}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P85515}.
CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P61163}.
CC -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily. {ECO:0000305}.
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DR EMBL; AB010297; BAA24423.1; -; mRNA.
DR EMBL; AK010632; BAB27076.1; -; mRNA.
DR EMBL; AK088062; BAC40124.1; -; mRNA.
DR EMBL; AK167450; BAE39536.1; -; mRNA.
DR EMBL; AK168889; BAE40706.1; -; mRNA.
DR EMBL; BC007131; AAH07131.1; -; mRNA.
DR CCDS; CCDS29878.1; -.
DR RefSeq; NP_058556.1; NM_016860.1.
DR AlphaFoldDB; P61164; -.
DR SMR; P61164; -.
DR BioGRID; 207569; 32.
DR IntAct; P61164; 19.
DR MINT; P61164; -.
DR STRING; 10090.ENSMUSP00000039844; -.
DR iPTMnet; P61164; -.
DR PhosphoSitePlus; P61164; -.
DR SwissPalm; P61164; -.
DR REPRODUCTION-2DPAGE; P61164; -.
DR EPD; P61164; -.
DR jPOST; P61164; -.
DR MaxQB; P61164; -.
DR PaxDb; P61164; -.
DR PeptideAtlas; P61164; -.
DR PRIDE; P61164; -.
DR ProteomicsDB; 285723; -.
DR Antibodypedia; 31450; 279 antibodies from 32 providers.
DR DNASU; 54130; -.
DR Ensembl; ENSMUST00000040270; ENSMUSP00000039844; ENSMUSG00000025228.
DR GeneID; 54130; -.
DR KEGG; mmu:54130; -.
DR UCSC; uc008htm.1; mouse.
DR CTD; 10121; -.
DR MGI; MGI:1858964; Actr1a.
DR VEuPathDB; HostDB:ENSMUSG00000025228; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000155782; -.
DR HOGENOM; CLU_027965_0_1_1; -.
DR InParanoid; P61164; -.
DR OMA; CIHSRFM; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P61164; -.
DR TreeFam; TF300420; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 54130; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Actr1a; mouse.
DR PRO; PR:P61164; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P61164; protein.
DR Bgee; ENSMUSG00000025228; Expressed in ear vesicle and 260 other tissues.
DR ExpressionAtlas; P61164; baseline and differential.
DR Genevisible; P61164; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0030137; C:COPI-coated vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0002177; C:manchette; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..376
FT /note="Alpha-centractin"
FT /id="PRO_0000089059"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61163"
SQ SEQUENCE 376 AA; 42614 MW; 4A978E7AB3739436 CRC64;
MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP
KAEEHRGLLS IRYPMEHGIV KDWNDMERIW QYVYSKDQLQ TFSEEHPVLL TEAPLNPRKN
RERAAEVFFE TFNVPALFIS MQAVLSLYAT GRTTGVVLDS GDGVTHAVPI YEGFAMPHSI
MRIDIAGRDV SRFLRLYLRK EGYDFHSSSE FEIVKAIKER ACYLSINPQK DETLETEKAQ
YYLPDGSTIE IGPSRFRAPE LLFRPDLIGE ESEGIHEVLV FAIQKSDMDL RRTLFSNIVL
SGGSTLFKGF GDRLLSEVKK LAPKDVKIRI SAPQERLYST WIGGSILASL DTFKKMWVSK
KEYEEDGARS IHRKTF
