ID   SPIR1_HUMAN             Reviewed;         756 AA.
AC   Q08AE8; Q1RMD4; Q9NQ71; Q9ULT4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   07-JUL-2009, entry version 25.
DE   RecName: Full=Protein spire homolog 1;
DE            Short=Spir-1;
GN   Name=SPIRE1; Synonyms=KIAA1135, SPIR1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=20039618; PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis
RT   from size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [2]
RP   SEQUENCE REVISION.
RX   MEDLINE=22158633; PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA   Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA   Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA   Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA   Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA   Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA   O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-756 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-756 (ISOFORM 1).
RC   TISSUE=Embryonic stem cell;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 123-756 (ISOFORM 2), FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Brain, and Testis;
RX   MEDLINE=21614650; PubMed=11747823; DOI=10.1016/S0960-9822(01)00602-9;
RA   Kerkhoff E., Simpson J.C., Leberfinger C.B., Otto I.M., Doerks T.,
RA   Bork P., Rapp U.R., Raabe T., Pepperkok R.;
RT   "The Spir actin organizers are involved in vesicle transport
RT   processes.";
RL   Curr. Biol. 11:1963-1968(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-465 AND
RP   SER-467, AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-465 AND
RP   SER-467, AND MASS SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- FUNCTION: Acts as a actin nucleation factor, remains associated
CC       with the slow-growing pointed end of the new filament. Involved in
CC       vesicle transport processes providing a novel link between actin
CC       organization and intracellular transport.
CC   -!- INTERACTION:
CC       P27348:YWHAQ; NbExp=1; IntAct=EBI-1055655, EBI-359854;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC       perinuclear region. Note=Punctate spots in perinuclear region and
CC       cytoplasm, co-localised with Rab11.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q08AE8-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q08AE8-2; Sequence=VSP_052595;
CC   -!- DOMAIN: Binds to actin monomers via the WH2 domain (By
CC       similarity).
CC   -!- DOMAIN: The Spir-box targets binding to intracellular membrane
CC       structures.
CC   -!- SIMILARITY: Belongs to the spire family.
CC   -!- SIMILARITY: Contains 1 KIND domain.
CC   -!- SIMILARITY: Contains 2 WH2 domains.
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DR   EMBL; AB032961; BAA86449.2; ALT_INIT; mRNA.
DR   EMBL; AP005482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC115005; AAI15006.1; ALT_INIT; mRNA.
DR   EMBL; BC125206; AAI25207.1; ALT_INIT; mRNA.
DR   EMBL; BC125207; AAI25208.1; ALT_INIT; mRNA.
DR   EMBL; AJ277587; CAB96370.1; ALT_INIT; mRNA.
DR   IPI; IPI00171145; -.
DR   IPI; IPI00645268; -.
DR   RefSeq; NP_001122098.1; -.
DR   RefSeq; NP_001122099.1; -.
DR   RefSeq; NP_064533.3; -.
DR   UniGene; Hs.515283; -.
DR   IntAct; Q08AE8; 1.
DR   PhosphoSite; Q08AE8; -.
DR   PRIDE; Q08AE8; -.
DR   Ensembl; ENSG00000134278; Homo sapiens.
DR   GeneID; 56907; -.
DR   KEGG; hsa:56907; -.
DR   UCSC; uc002krd.1; human.
DR   UCSC; uc002kre.1; human.
DR   GeneCards; GC18M012438; -.
DR   HGNC; HGNC:30622; SPIRE1.
DR   MIM; 609216; gene.
DR   HOVERGEN; Q08AE8; -.
DR   NextBio; 62379; -.
DR   Bgee; Q08AE8; -.
DR   CleanEx; HS_SPIRE1; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011019; KIND.
DR   PROSITE; PS51377; KIND; 1.
DR   PROSITE; PS51082; WH2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Coiled coil; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Repeat; Transport.
FT   CHAIN         1    756       Protein spire homolog 1.
FT                                /FTId=PRO_0000309569.
FT   DOMAIN       40    231       KIND.
FT   DOMAIN      305    323       WH2 1.
FT   DOMAIN      369    386       WH2 2.
FT   REGION      556    576       Spir-box.
FT   COILED      229    257       Potential.
FT   MOD_RES     464    464       Phosphoserine.
FT   MOD_RES     465    465       Phosphoserine.
FT   MOD_RES     467    467       Phosphoserine.
FT   VAR_SEQ     397    410       Missing (in isoform 2).
FT                                /FTId=VSP_052595.
FT   CONFLICT    410    410       P -> S (in Ref. 1; BAA86449 and 4;
FT                                AAI25207).
SQ   SEQUENCE   756 AA;  85554 MW;  0B83C3B1BC852040 CRC64;
     MAQAAGPAGG GEPRTEAVGG EGPREPGAAG GAAGGSRDAL SLEEILRLYN QPINEEQAWA
     VCYQCCGSLR AAARRRQPRH RVRSAAQIRV WRDGAVTLAP AADDAGEPPP VAGKLGYSQC
     METEVIESLG IIIYKALDYG LKENEERELS PPLEQLIDHM ANTVEADGSN DEGYEAAEEG
     LGDEDEKRKI SAIRSYRDVM KLCAAHLPTE SDAPNHYQAV CRALFAETME LHTFLTKIKS
     AKENLKKIQE MEKSDESSTD LEELKNADWA RFWVQVMRDL RNGVKLKKVQ ERQYNPLPIE
     YQLTPYEMLM DDIRCKRYTL RKVMVNGDIP PRLKKSAHEI ILDFIRSRPP LNPVSARKLK
     PTPPRPRSLH ERILEEIKAE RKLRPVSPEE IRRSRLAMRP LSMSYSFDLP DVTTPESTKN
     LVESSMVNGG LTSQTKENGL STSQQVPAQR KKLLRAPTLA ELDSSESEEE TLHKSTSSSS
     VSPSFPEEPV LEAVSTRKKP PKFLPISSTP QPERRQPPQR RHSIEKETPT NVRQFLPPSR
     QSSRSLEEFC YPVECLALTV EEVMHIRQVL VKAELEKYQQ YKDIYTALKK GKLCFCCRTR
     RFSFFTWSYT CQFCKRPVCS QCCKKMRLPS KPYSTLPIFS LGPSALQRGE SSMRSEKPST
     AHHRPLRSIA RFSSKSKSMD KSDEELQFPK ELMEDWSTME VCVDCKKFIS EIISSSRRSL
     VLANKRARLK RKTQSFYMSS PGPSEYCPSE RTISEI
//