SPIR1_MOUSE
ID SPIR1_MOUSE Reviewed; 598 AA.
AC Q52KF3; Q6PDJ5; Q80V45;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein spire homolog 1;
GN Name=Spire1 {ECO:0000312|MGI:MGI:1915416};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 314-598 (ISOFORM 3).
RC STRAIN=129, and C57BL/6J {ECO:0000312|EMBL:AAH94375.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH94375.1}, and 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 [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15053972; DOI=10.1016/j.modgep.2003.11.006;
RA Schumacher N., Borawski J.M., Leberfinger C.B., Gessler M., Kerkhoff E.;
RT "Overlapping expression pattern of the actin organizers Spir-1 and formin-2
RT in the developing mouse nervous system and the adult brain.";
RL Gene Expr. Patterns 4:249-255(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-305; SER-306;
RP SER-308; SER-520; SER-524 AND SER-577, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-248 AND SER-259 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21983562; DOI=10.1038/ncb2353;
RA Schuh M.;
RT "An actin-dependent mechanism for long-range vesicle transport.";
RL Nat. Cell Biol. 13:1431-1436(2011).
CC -!- FUNCTION: Acts as an actin nucleation factor, remains associated with
CC the slow-growing pointed end of the new filament (PubMed:21620703,
CC PubMed:21983562). Involved in intracellular vesicle transport along
CC actin fibers, providing a novel link between actin cytoskeleton
CC dynamics and intracellular transport (PubMed:21983562). Required for
CC asymmetric spindle positioning and asymmetric cell division during
CC oocyte 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). {ECO:0000269|PubMed:21620703,
CC ECO:0000269|PubMed:21983562}.
CC -!- SUBUNIT: Interacts with FMN2. {ECO:0000250|UniProtKB:Q08AE8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21983562}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. Cleavage
CC furrow {ECO:0000269|PubMed:21620703}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q08AE8}. Cell membrane
CC {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}; Peripheral
CC membrane protein {ECO:0000269|PubMed:21620703,
CC ECO:0000269|PubMed:21983562}; Cytoplasmic side
CC {ECO:0000269|PubMed:21620703, ECO:0000269|PubMed:21983562}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:21983562}; Peripheral membrane
CC protein {ECO:0000269|PubMed:21983562}; Cytoplasmic side
CC {ECO:0000269|PubMed:21983562}. Note=Punctate spots in perinuclear
CC region and cytoplasm, co-localized with Rab11 (PubMed:21983562).
CC Detected at the cleavage furrow during asymmetric oocyte division and
CC polar body extrusion (PubMed:21620703). {ECO:0000269|PubMed:21620703,
CC ECO:0000269|PubMed:21983562}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q52KF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q52KF3-2; Sequence=VSP_052596;
CC Name=3;
CC IsoId=Q52KF3-3; Sequence=VSP_038300;
CC -!- TISSUE SPECIFICITY: Expressed in the developing nervous system and in
CC the adult brain, specifically the Purkinje cells of the cerebellum, in
CC neuronal cells in the CA1, CA2 and CA3 fields of the hippocampus and
CC granular layer of the dentate gyrus (PubMed:15053972). Detected in
CC oocytes (PubMed:21620703). {ECO:0000269|PubMed:15053972,
CC ECO:0000269|PubMed:21620703}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults.
CC {ECO:0000269|PubMed:15053972}.
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:0000250|UniProtKB:Q08AE8}.
CC -!- SIMILARITY: Belongs to the spire family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58669.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC046486; AAH46486.2; -; mRNA.
DR EMBL; BC058669; AAH58669.1; ALT_INIT; mRNA.
DR EMBL; BC094375; AAH94375.1; -; mRNA.
DR AlphaFoldDB; Q52KF3; -.
DR SMR; Q52KF3; -.
DR IntAct; Q52KF3; 1.
DR MINT; Q52KF3; -.
DR iPTMnet; Q52KF3; -.
DR PhosphoSitePlus; Q52KF3; -.
DR SwissPalm; Q52KF3; -.
DR MaxQB; Q52KF3; -.
DR PRIDE; Q52KF3; -.
DR ProteomicsDB; 258722; -. [Q52KF3-1]
DR ProteomicsDB; 258723; -. [Q52KF3-2]
DR ProteomicsDB; 258724; -. [Q52KF3-3]
DR Antibodypedia; 21944; 95 antibodies from 20 providers.
DR Ensembl; ENSMUST00000082243; ENSMUSP00000080871; ENSMUSG00000024533. [Q52KF3-1]
DR UCSC; uc008fmn.1; mouse. [Q52KF3-2]
DR UCSC; uc012bej.1; mouse. [Q52KF3-1]
DR MGI; MGI:1915416; Spire1.
DR VEuPathDB; HostDB:ENSMUSG00000024533; -.
DR GeneTree; ENSGT00390000003058; -.
DR InParanoid; Q52KF3; -.
DR OMA; GPPRMCT; -.
DR PhylomeDB; Q52KF3; -.
DR ChiTaRS; Spire1; mouse.
DR PRO; PR:Q52KF3; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q52KF3; protein.
DR Bgee; ENSMUSG00000024533; Expressed in secondary oocyte and 230 other tissues.
DR ExpressionAtlas; Q52KF3; baseline and differential.
DR Genevisible; Q52KF3; MM.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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: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:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0036089; P:cleavage furrow formation; IMP:UniProtKB.
DR GO; GO:0060996; P:dendritic spine development; IMP:MGI.
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; IDA:MGI.
DR GO; GO:0046907; P:intracellular transport; IMP:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISO:MGI.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP: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 SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51377; KIND; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..598
FT /note="Protein spire homolog 1"
FT /id="PRO_0000309571"
FT DOMAIN 1..73
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 147..165
FT /note="WH2 1"
FT /evidence="ECO:0000255"
FT DOMAIN 211..228
FT /note="WH2 2"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..418
FT /note="Spir-box"
FT REGION 488..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AE8"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AE8"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 238
FT /note="L -> LA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052596"
FT VAR_SEQ 388
FT /note="L -> LVPRITGVWPRTPFRPLFSTIQTASLLSSHPFEAAMFGVAGAMYYLF
FT ERAFTSRWKPSK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038300"
FT MOD_RES Q52KF3-2:248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q52KF3-2:259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 598 AA; 68450 MW; 3E0D490F47CF568B CRC64;
MANTVEADGS KDEGYEAADE GPEDEDGEKR SISAIRSYQD VMKICAAHLP TESEAPNHYQ
AVCRALFAET MELHTFLTKI KSAKENLKKI QEMEKGDESS TDLEDLKNAD WARFWVQVMR
DLRNGVKLKK VQQRQYNPLP IEYQLTPYEM LMDDIRCKRY TLRKVMVNGD VPPRLKKSAH
EVILDFIRSR PPLNPVSARK LKPTPPRPRS LHERILEEIK AERKLRPVSP EEIRRSRLVR
PLSMSHSFDL SDVTTPESPK NVGESSMVNG GLTSQTKENG LSAAQQGSAQ RKRLLKAPTL
AELDSSDSEE EKSLHKSTSS SSASPSLYED PVLEAMCSRK KPPKFLPISS TPQPERRQPP
QRRHSIEKET PTNVRQFLPP SRQSSRSLEE FCYPVECLAL TVEEVMHIRQ VLVKAELEKY
QQYKDVYTAL KKGKLCFCCR TRRFSFFTWS YTCQFCKRPV CSQCCKKMRL PSKPYSTLPI
FSLGPSALQR GESCSRSEKP STSHHRPLRS IARFSTKSRS VDKSDEELQF PKELMEDWST
MEVCVDCKKF ISEIISSSRR SLVLANKRAR LKRKTQSFYM SSAGPSEYCP SERTINEI
