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ACTZ_HUMAN
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   03-AUG-2022, entry version 172.
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   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: Component of a multi-subunit complex involved in microtubule
CC       based vesicle motility. It is associated with the centrosome.
CC   -!- SUBUNIT: Interacts with BCCIP (isoform 2/alpha).
CC       {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}.
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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; 193.
DR   IntAct; P61163; 62.
DR   MINT; P61163; -.
DR   STRING; 9606.ENSP00000358921; -.
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   UCD-2DPAGE; P61163; -.
DR   EPD; P61163; -.
DR   jPOST; P61163; -.
DR   MassIVE; P61163; -.
DR   MaxQB; P61163; -.
DR   PaxDb; P61163; -.
DR   PeptideAtlas; P61163; -.
DR   PRIDE; P61163; -.
DR   ProteomicsDB; 57270; -.
DR   Antibodypedia; 31450; 279 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   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; 649708at2759; -.
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; 525 hits in 1091 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 210 other tissues.
DR   ExpressionAtlas; P61163; baseline and differential.
DR   Genevisible; P61163; HS.
DR   GO; GO:0099738; C:cell cortex region; 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   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;
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
 
 
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