SPIR1_HUMAN
ID SPIR1_HUMAN Reviewed; 756 AA.
AC Q08AE8; A8K2B5; J3KQ50; J3KQR5; Q1RMD4; Q8NDP1; Q9NQ71; Q9ULT4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein spire homolog 1;
DE Short=Spir-1;
GN Name=SPIRE1 {ECO:0000312|EMBL:AAI25207.1}; Synonyms=KIAA1135, SPIR1;
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] {ECO:0000305, ECO:0000312|EMBL:BAA86449.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAA86449.2};
RX 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 from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [2]
RP SEQUENCE REVISION.
RX 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 MRNA] (ISOFORM 3).
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 MRNA] (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5] {ECO:0000305}
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., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., 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 [6]
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 [7] {ECO:0000305, ECO:0000312|EMBL:AAI25207.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-756 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-756 (ISOFORMS 1 AND 2).
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:AAI15006.1};
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 [8] {ECO:0000305, ECO:0000312|EMBL:CAB96370.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 123-756 (ISOFORM 2), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain {ECO:0000312|EMBL:CAB96370.1}, and
RC Testis {ECO:0000312|EMBL:CAB96370.1};
RX PubMed=11747823; DOI=10.1016/s0960-9822(01)00602-9;
RA Kerkhoff E., Simpson J.C., Leberfinger C.B., Otto I.M., Doerks T., Bork P.,
RA Rapp U.R., Raabe T., Pepperkok R.;
RT "The Spir actin organizers are involved in vesicle transport processes.";
RL Curr. Biol. 11:1963-1968(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-465 AND SER-467, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
RN [10]
RP FUNCTION.
RX PubMed=21620703; DOI=10.1016/j.cub.2011.04.029;
RA Pfender S., Kuznetsov V., Pleiser S., Kerkhoff E., Schuh M.;
RT "Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric
RT oocyte division.";
RL Curr. Biol. 21:955-960(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; THR-509 AND SER-678, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP FUNCTION.
RX PubMed=26287480; DOI=10.7554/elife.07735;
RA Belin B.J., Lee T., Mullins R.D.;
RT "DNA damage induces nuclear actin filament assembly by Formin -2 and Spire-
RT 1/2 that promotes efficient DNA repair.";
RL Elife 4:E07735-E07735(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-236 IN COMPLEX WITH FMN2,
RP INTERACTION WITH FMN2, AND MUTAGENESIS OF TYR-134 AND ASP-138.
RX PubMed=21705804; DOI=10.1074/jbc.m111.257782;
RA Zeth K., Pechlivanis M., Samol A., Pleiser S., Vonrhein C., Kerkhoff E.;
RT "Molecular basis of actin nucleation factor cooperativity: crystal
RT structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2
RT formin SPIR interaction motif (FSI) complex.";
RL J. Biol. Chem. 286:30732-30739(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-237 IN COMPLEX WITH FMN2,
RP INTERACTION WITH FMN2, AND MUTAGENESIS OF ILE-131; ASP-138 AND GLU-146.
RX PubMed=21730168; DOI=10.1073/pnas.1105703108;
RA Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W.,
RA Quinlan M.E., Eck M.J.;
RT "Structure and function of the interacting domains of Spire and Fmn-family
RT formins.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011).
CC -!- FUNCTION: Acts as an actin nucleation factor, remains associated with
CC the slow-growing pointed end of the new filament (PubMed:11747823,
CC PubMed:21620703). Involved in intracellular vesicle transport along
CC actin fibers, providing a novel link between actin cytoskeleton
CC dynamics and intracellular transport (PubMed:11747823). Required for
CC asymmetric spindle positioning and asymmetric cell division during
CC meiosis (PubMed:21620703). Required for normal formation of the
CC cleavage furrow and for polar body extrusion during female germ cell
CC meiosis (PubMed:21620703). Also acts in the nucleus: together with
CC FMN2, promotes assembly of nuclear actin filaments in response to DNA
CC damage in order to facilitate movement of chromatin and repair factors
CC after DNA damage (PubMed:26287480). {ECO:0000269|PubMed:11747823,
CC ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:26287480}.
CC -!- SUBUNIT: Interacts with FMN2. {ECO:0000269|PubMed:21705804,
CC ECO:0000269|PubMed:21730168}.
CC -!- INTERACTION:
CC Q08AE8; P13637: ATP1A3; NbExp=3; IntAct=EBI-1055655, EBI-948169;
CC Q08AE8; Q96RK4: BBS4; NbExp=3; IntAct=EBI-1055655, EBI-1805814;
CC Q08AE8; P16284: PECAM1; NbExp=3; IntAct=EBI-1055655, EBI-716404;
CC Q08AE8; Q13393: PLD1; NbExp=3; IntAct=EBI-1055655, EBI-2827556;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11747823}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11747823}. Cell membrane
CC {ECO:0000269|PubMed:11747823}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11747823}; Cytoplasmic side
CC {ECO:0000269|PubMed:11747823}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q52KF3}. Note=Detected at the cleavage furrow
CC during asymmetric oocyte division and polar body extrusion (By
CC similarity). Punctate spots in perinuclear region and cytoplasm,
CC colocalized with Rab11 (By similarity). {ECO:0000250|UniProtKB:Q52KF3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=Q08AE8-1; Sequence=Displayed;
CC Name=5;
CC IsoId=Q08AE8-5; Sequence=VSP_054464, VSP_052595;
CC Name=2 {ECO:0000269|PubMed:11747823, ECO:0000269|PubMed:15489334};
CC IsoId=Q08AE8-2; Sequence=VSP_052595;
CC Name=3;
CC IsoId=Q08AE8-3; Sequence=VSP_037925, VSP_052595;
CC Name=4;
CC IsoId=Q08AE8-4; Sequence=VSP_037925, VSP_052595, VSP_037926;
CC -!- DOMAIN: Binds to actin monomers via the WH2 domain.
CC {ECO:0000250|UniProtKB:Q9U1K1}.
CC -!- DOMAIN: The Spir-box targets binding to intracellular membrane
CC structures. {ECO:0000269|PubMed:11747823}.
CC -!- SIMILARITY: Belongs to the spire family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI15006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI25207.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI25208.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA86449.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB032961; BAA86449.2; ALT_INIT; mRNA.
DR EMBL; AK290180; BAF82869.1; -; mRNA.
DR EMBL; AL833817; CAD38680.1; -; mRNA.
DR EMBL; AP001028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01546.1; -; 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; -; mRNA.
DR CCDS; CCDS32790.2; -. [Q08AE8-2]
DR CCDS; CCDS45829.1; -. [Q08AE8-1]
DR CCDS; CCDS45830.1; -. [Q08AE8-5]
DR RefSeq; NP_001122098.1; NM_001128626.1. [Q08AE8-1]
DR RefSeq; NP_001122099.1; NM_001128627.1. [Q08AE8-5]
DR RefSeq; NP_064533.3; NM_020148.2. [Q08AE8-2]
DR PDB; 2YLE; X-ray; 1.80 A; A=36-236.
DR PDB; 2YLF; X-ray; 2.05 A; A=36-236.
DR PDB; 3R7G; X-ray; 2.20 A; A=20-237.
DR PDB; 3RBW; X-ray; 3.20 A; A/B/C/D=20-237.
DR PDBsum; 2YLE; -.
DR PDBsum; 2YLF; -.
DR PDBsum; 3R7G; -.
DR PDBsum; 3RBW; -.
DR AlphaFoldDB; Q08AE8; -.
DR SMR; Q08AE8; -.
DR BioGRID; 121237; 23.
DR DIP; DIP-42378N; -.
DR IntAct; Q08AE8; 18.
DR MINT; Q08AE8; -.
DR STRING; 9606.ENSP00000387266; -.
DR iPTMnet; Q08AE8; -.
DR PhosphoSitePlus; Q08AE8; -.
DR BioMuta; SPIRE1; -.
DR DMDM; 425906061; -.
DR EPD; Q08AE8; -.
DR jPOST; Q08AE8; -.
DR MassIVE; Q08AE8; -.
DR MaxQB; Q08AE8; -.
DR PaxDb; Q08AE8; -.
DR PeptideAtlas; Q08AE8; -.
DR PRIDE; Q08AE8; -.
DR ProteomicsDB; 58658; -. [Q08AE8-1]
DR ProteomicsDB; 58659; -. [Q08AE8-2]
DR ProteomicsDB; 58660; -. [Q08AE8-3]
DR ProteomicsDB; 58661; -. [Q08AE8-4]
DR Antibodypedia; 21944; 95 antibodies from 20 providers.
DR DNASU; 56907; -.
DR Ensembl; ENST00000409402.9; ENSP00000387266.3; ENSG00000134278.16. [Q08AE8-1]
DR Ensembl; ENST00000410092.7; ENSP00000387226.3; ENSG00000134278.16. [Q08AE8-2]
DR Ensembl; ENST00000440472.6; ENSP00000404752.1; ENSG00000134278.16. [Q08AE8-4]
DR Ensembl; ENST00000453447.6; ENSP00000407050.1; ENSG00000134278.16. [Q08AE8-5]
DR GeneID; 56907; -.
DR KEGG; hsa:56907; -.
DR MANE-Select; ENST00000409402.9; ENSP00000387266.3; NM_001128626.2; NP_001122098.1.
DR UCSC; uc002kre.4; human. [Q08AE8-1]
DR CTD; 56907; -.
DR DisGeNET; 56907; -.
DR GeneCards; SPIRE1; -.
DR HGNC; HGNC:30622; SPIRE1.
DR HPA; ENSG00000134278; Low tissue specificity.
DR MIM; 609216; gene.
DR neXtProt; NX_Q08AE8; -.
DR OpenTargets; ENSG00000134278; -.
DR PharmGKB; PA134895885; -.
DR VEuPathDB; HostDB:ENSG00000134278; -.
DR eggNOG; ENOG502QQPN; Eukaryota.
DR GeneTree; ENSGT00390000003058; -.
DR HOGENOM; CLU_018839_1_1_1; -.
DR InParanoid; Q08AE8; -.
DR OMA; GPPRMCT; -.
DR OrthoDB; 560461at2759; -.
DR PhylomeDB; Q08AE8; -.
DR TreeFam; TF326239; -.
DR PathwayCommons; Q08AE8; -.
DR SignaLink; Q08AE8; -.
DR BioGRID-ORCS; 56907; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; SPIRE1; human.
DR GenomeRNAi; 56907; -.
DR Pharos; Q08AE8; Tbio.
DR PRO; PR:Q08AE8; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q08AE8; protein.
DR Bgee; ENSG00000134278; Expressed in ganglionic eminence and 191 other tissues.
DR ExpressionAtlas; Q08AE8; baseline and differential.
DR Genevisible; Q08AE8; HS.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:CACAO.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0036089; P:cleavage furrow formation; ISS:UniProtKB.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IMP:UniProtKB.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IMP:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; ISS:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; ISS:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:CACAO.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR029901; Spire.
DR InterPro; IPR029905; Spire1.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR21345; PTHR21345; 1.
DR PANTHER; PTHR21345:SF8; PTHR21345:SF8; 1.
DR Pfam; PF16474; KIND; 1.
DR SMART; SM00750; KIND; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51377; KIND; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell membrane; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..756
FT /note="Protein spire homolog 1"
FT /id="PRO_0000309569"
FT DOMAIN 40..231
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 305..323
FT /note="WH2 1"
FT DOMAIN 369..386
FT /note="WH2 2"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..138
FT /note="Important for interaction with FMN2"
FT REGION 425..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..576
FT /note="Spir-box"
FT COILED 229..257
FT /evidence="ECO:0000255"
FT COMPBIAS 425..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52KF3"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52KF3"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52KF3"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_037925"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_054464"
FT VAR_SEQ 397..410
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:11747823,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_052595"
FT VAR_SEQ 616..756
FT /note="RPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESSMRSEKPSTAHHRPLR
FT SIARFSSKSKSMDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKR
FT ARLKRKTQSFYMSSPGPSEYCPSERTISEI -> SDCLFNGTAHCQFYLG (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_037926"
FT VARIANT 249
FT /note="Q -> P (in dbSNP:rs1785296)"
FT /id="VAR_058695"
FT MUTAGEN 131
FT /note="I->K: Strongly reduces interaction with FMN2."
FT /evidence="ECO:0000269|PubMed:21730168"
FT MUTAGEN 134
FT /note="Y->K: Abolishes interaction with FMN2."
FT /evidence="ECO:0000269|PubMed:21705804"
FT MUTAGEN 138
FT /note="D->N: Abolishes interaction with FMN2."
FT /evidence="ECO:0000269|PubMed:21705804,
FT ECO:0000269|PubMed:21730168"
FT MUTAGEN 146
FT /note="E->A,K: Abolishes interaction with FMN2."
FT /evidence="ECO:0000269|PubMed:21730168"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 55..74
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2YLE"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2YLE"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2YLE"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:2YLE"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2YLE"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:2YLE"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 213..234
FT /evidence="ECO:0007829|PDB:2YLE"
SQ SEQUENCE 756 AA; 85544 MW; 1379B39C8CA9DDB3 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 LSMSYSFDLS 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
