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   24-JAN-2024, entry version 161.
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,
RC   Pancreas, 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: Part of the ACTR1A/ACTB filament around which the dynactin
CC       complex is built. The dynactin multiprotein complex activates the
CC       molecular motor dynein for ultra-processive transport along
CC       microtubules. {ECO:0000250|UniProtKB:F2Z5G5}.
CC   -!- SUBUNIT: Part of the ACTR1A/ACTB filament around which the dynactin
CC       complex is built. The filament contains 8 copies of ACTR1A and 1 ACTB.
CC       Interacts with dynein and adapters such as BICD2 (By similarity).
CC       Interacts with BCCIP (isoform 2/alpha) (By similarity).
CC       {ECO:0000250|UniProtKB:F2Z5G5, ECO:0000250|UniProtKB:P61163}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P85515}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:P61163}.
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; 33.
DR   IntAct; P61164; 19.
DR   MINT; P61164; -.
DR   STRING; 10090.ENSMUSP00000039844; -.
DR   GlyGen; P61164; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61164; -.
DR   PhosphoSitePlus; P61164; -.
DR   SwissPalm; P61164; -.
DR   REPRODUCTION-2DPAGE; P61164; -.
DR   EPD; P61164; -.
DR   jPOST; P61164; -.
DR   MaxQB; P61164; -.
DR   PaxDb; 10090-ENSMUSP00000039844; -.
DR   PeptideAtlas; P61164; -.
DR   ProteomicsDB; 285723; -.
DR   Pumba; P61164; -.
DR   Antibodypedia; 31450; 294 antibodies from 32 providers.
DR   DNASU; 54130; -.
DR   Ensembl; ENSMUST00000040270.6; ENSMUSP00000039844.5; ENSMUSG00000025228.6.
DR   GeneID; 54130; -.
DR   KEGG; mmu:54130; -.
DR   UCSC; uc008htm.1; mouse.
DR   AGR; MGI:1858964; -.
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; 10at2759; -.
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 78 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 263 other cell types or tissues.
DR   ExpressionAtlas; P61164; baseline and differential.
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   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF370; ALPHA-CENTRACTIN; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
DR   Genevisible; P61164; MM.
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
//