ID ACTZ_HUMAN Reviewed; 376 AA. AC P61163; B2R6B0; P42024; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 1. DT 27-MAR-2024, entry version 181. 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 {ECO:0000312|HGNC:HGNC:167}; Synonyms=CTRN1; 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]. RX PubMed=7696711; DOI=10.1091/mbc.5.12.1301; RA Clark S.W., Staub O., Holzbaur E.L.F., Paschal B.M., Vallee R.B., RA Meyer D.I., Clark I.B.; RT "Beta-centractin: characterization and distribution of a new member of the RT centractin family of actin-related proteins."; RL Mol. Biol. Cell 5:1301-1310(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX PubMed=1528266; DOI=10.1038/359244a0; RA Lees-Miller J.P., Helfman D.M., Schroer T.A.; RT "A vertebrate actin-related protein is a component of a multisubunit RT complex involved in microtubule-based vesicle motility."; RL Nature 359:244-246(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thalamus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Muscle; 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 [7] RP PROTEIN SEQUENCE OF 1-22; 239-255 AND 330-336, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Osteosarcoma; RA Bienvenut W.V., Glen H., Frame M.C.; RL Submitted (MAR-2008) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 97-118; 201-215 AND 239-255, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=22327364; DOI=10.1038/ncb2440; RA Kiyomitsu T., Cheeseman I.M.; RT "Chromosome- and spindle-pole-derived signals generate an intrinsic code RT for spindle position and orientation."; RL Nat. Cell Biol. 14:311-317(2012). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [16] RP INTERACTION WITH BCCIP. RX PubMed=28394342; DOI=10.1038/onc.2017.92; RA Huhn S.C., Liu J., Ye C., Lu H., Jiang X., Feng X., Ganesan S., White E., RA Shen Z.; RT "Regulation of spindle integrity and mitotic fidelity by BCCIP."; RL Oncogene 36:4750-4766(2017). 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) (PubMed:28394342). CC {ECO:0000250|UniProtKB:F2Z5G5, ECO:0000269|PubMed:28394342}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P85515}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, CC cell cortex {ECO:0000269|PubMed:22327364}. CC -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X82206; CAA57690.1; -; mRNA. DR EMBL; Z14978; CAA78701.1; -; mRNA. DR EMBL; AK312506; BAG35407.1; -; mRNA. DR EMBL; AL121928; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49685.1; -; Genomic_DNA. DR EMBL; BC000693; AAH00693.1; -; mRNA. DR EMBL; BC026016; AAH26016.1; -; mRNA. DR CCDS; CCDS7536.1; -. DR PIR; S29089; S29089. DR RefSeq; NP_005727.1; NM_005736.3. DR AlphaFoldDB; P61163; -. DR SMR; P61163; -. DR BioGRID; 115425; 269. DR IntAct; P61163; 65. DR MINT; P61163; -. DR STRING; 9606.ENSP00000358921; -. DR GlyGen; P61163; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61163; -. DR MetOSite; P61163; -. DR PhosphoSitePlus; P61163; -. DR SwissPalm; P61163; -. DR BioMuta; ACTR1A; -. DR DMDM; 47117651; -. DR OGP; P42024; -. DR REPRODUCTION-2DPAGE; IPI00029468; -. DR EPD; P61163; -. DR jPOST; P61163; -. DR MassIVE; P61163; -. DR MaxQB; P61163; -. DR PaxDb; 9606-ENSP00000358921; -. DR PeptideAtlas; P61163; -. DR ProteomicsDB; 57270; -. DR Pumba; P61163; -. DR Antibodypedia; 31450; 294 antibodies from 32 providers. DR DNASU; 10121; -. DR Ensembl; ENST00000369905.9; ENSP00000358921.4; ENSG00000138107.13. DR GeneID; 10121; -. DR KEGG; hsa:10121; -. DR MANE-Select; ENST00000369905.9; ENSP00000358921.4; NM_005736.4; NP_005727.1. DR UCSC; uc001kvv.4; human. DR AGR; HGNC:167; -. DR CTD; 10121; -. DR DisGeNET; 10121; -. DR GeneCards; ACTR1A; -. DR HGNC; HGNC:167; ACTR1A. DR HPA; ENSG00000138107; Low tissue specificity. DR MIM; 605143; gene. DR neXtProt; NX_P61163; -. DR OpenTargets; ENSG00000138107; -. DR PharmGKB; PA24486; -. DR VEuPathDB; HostDB:ENSG00000138107; -. DR eggNOG; KOG0676; Eukaryota. DR GeneTree; ENSGT00940000155782; -. DR HOGENOM; CLU_027965_0_1_1; -. DR InParanoid; P61163; -. DR OMA; CIHSRFM; -. DR OrthoDB; 10at2759; -. DR PhylomeDB; P61163; -. DR TreeFam; TF300420; -. DR PathwayCommons; P61163; -. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-8854518; AURKA Activation by TPX2. DR SignaLink; P61163; -. DR BioGRID-ORCS; 10121; 557 hits in 1172 CRISPR screens. DR ChiTaRS; ACTR1A; human. DR GeneWiki; ACTR1A; -. DR GenomeRNAi; 10121; -. DR Pharos; P61163; Tbio. DR PRO; PR:P61163; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P61163; Protein. DR Bgee; ENSG00000138107; Expressed in cortical plate and 212 other cell types or tissues. DR ExpressionAtlas; P61163; baseline and differential. DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005869; C:dynactin complex; TAS:ProtInc. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc. 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 UCD-2DPAGE; P61163; -. DR Genevisible; P61163; HS. PE 1: Evidence at protein level; KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Nucleotide-binding; Reference proteome. FT CHAIN 1..376 FT /note="Alpha-centractin" FT /id="PRO_0000089058" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" 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 //