SPIR2_MOUSE
ID SPIR2_MOUSE Reviewed; 718 AA.
AC Q8K1S6; Q8R0R2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein spire homolog 2;
DE Short=Spir-2;
GN Name=Spire2; Synonyms=spir-2;
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 [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, Colon, and Eye;
RA Kerkhoff E., Leberfinger C.B., Borawski J.M., Rapp U.R., Doerks T.,
RA Bork P.;
RT "The Spir protein family.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Olfactory epithelium;
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 [3]
RP SPIRE FAMILY.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [5]
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 [6]
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). Also acts in the nucleus: together with
CC SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in
CC response to DNA damage in order to facilitate movement of chromatin and
CC repair factors after DNA damage (By similarity).
CC {ECO:0000250|UniProtKB:Q8WWL2, ECO:0000269|PubMed:21620703,
CC ECO:0000269|PubMed:21983562}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21983562}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21983562}. Cell membrane
CC {ECO:0000269|PubMed:21983562}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21983562}; Cytoplasmic side
CC {ECO:0000269|PubMed:21983562}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:21983562}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21983562}; Cytoplasmic side
CC {ECO:0000269|PubMed:21983562}. Note=Detected at the cleavage furrow
CC during asymmetric oocyte division and polar body extrusion.
CC {ECO:0000269|PubMed:21620703}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K1S6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K1S6-2; Sequence=VSP_031573;
CC -!- TISSUE SPECIFICITY: Detected in oocytes. {ECO:0000269|PubMed:21620703}.
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}.
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DR EMBL; AJ459115; CAD30509.1; -; Genomic_DNA.
DR EMBL; BC026502; AAH26502.1; -; mRNA.
DR EMBL; BC049152; AAH49152.1; -; mRNA.
DR CCDS; CCDS22754.1; -. [Q8K1S6-1]
DR RefSeq; NP_758491.1; NM_172287.2. [Q8K1S6-1]
DR AlphaFoldDB; Q8K1S6; -.
DR SMR; Q8K1S6; -.
DR BioGRID; 231590; 33.
DR IntAct; Q8K1S6; 32.
DR STRING; 10090.ENSMUSP00000010298; -.
DR iPTMnet; Q8K1S6; -.
DR PhosphoSitePlus; Q8K1S6; -.
DR MaxQB; Q8K1S6; -.
DR PaxDb; Q8K1S6; -.
DR PRIDE; Q8K1S6; -.
DR ProteomicsDB; 261618; -. [Q8K1S6-1]
DR ProteomicsDB; 261619; -. [Q8K1S6-2]
DR Antibodypedia; 45052; 137 antibodies from 19 providers.
DR Ensembl; ENSMUST00000010298; ENSMUSP00000010298; ENSMUSG00000010154. [Q8K1S6-1]
DR Ensembl; ENSMUST00000212404; ENSMUSP00000148710; ENSMUSG00000010154. [Q8K1S6-2]
DR GeneID; 234857; -.
DR KEGG; mmu:234857; -.
DR UCSC; uc009nvj.1; mouse. [Q8K1S6-1]
DR CTD; 84501; -.
DR MGI; MGI:2446256; Spire2.
DR VEuPathDB; HostDB:ENSMUSG00000010154; -.
DR eggNOG; ENOG502QQPN; Eukaryota.
DR GeneTree; ENSGT00390000003058; -.
DR HOGENOM; CLU_018839_1_1_1; -.
DR InParanoid; Q8K1S6; -.
DR OMA; QWMEFSH; -.
DR OrthoDB; 560461at2759; -.
DR PhylomeDB; Q8K1S6; -.
DR TreeFam; TF326239; -.
DR BioGRID-ORCS; 234857; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q8K1S6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K1S6; protein.
DR Bgee; ENSMUSG00000010154; Expressed in forebrain ventricular layer and 160 other tissues.
DR Genevisible; Q8K1S6; MM.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
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; 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; IMP: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; 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; ISS:UniProtKB.
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; IPR029904; Spire2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR21345; PTHR21345; 1.
DR PANTHER; PTHR21345:SF5; PTHR21345:SF5; 1.
DR Pfam; PF16474; KIND; 1.
DR SMART; SM00750; KIND; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51377; KIND; 1.
DR PROSITE; PS51082; WH2; 2.
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..718
FT /note="Protein spire homolog 2"
FT /id="PRO_0000320024"
FT DOMAIN 26..207
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 251..265
FT /note="WH2 1"
FT DOMAIN 281..299
FT /note="WH2 2"
FT DOMAIN 345..362
FT /note="WH2 3"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..558
FT /note="Spir-box"
FT COMPBIAS 483..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWL2"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWL2"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWL2"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031573"
SQ SEQUENCE 718 AA; 80210 MW; 3D6B61292594E9B0 CRC64;
MARAGGGGAA APERAGGAAR PEPWELSLEE VLKVYEQPIN EEQAWAVCFQ GCRGLRGEPG
GVRRIRDTAD ILLRRDGSVG ARLEPEPTTM VVPPASSEAQ MVQSLGFAIY RALDWGLDEN
EERELSPQLE RLIDLMANSD CEDSSCGAAD EGYVGPEEEE EAEGGPRAVR TFAQAMRLCA
LRLTDPHGAQ AHYQAVCRAL FVETLELRAF LARVREAKEM LKKLGEEEPR EKPLAELDHL
GHTDWARLWV QLMRELRHGV KLKKVQEKEF NPLPTEFQLT PFEMLMQDIR ARNYKLRKVM
VDGDIPPRVK KDAHELILDF IRSRPPLKQV SERQLRPVPQ KQRTLHEKIL EEIKQERRLR
PVGAQHLGGR GFGSLPCILN ACSGDIKSTS CINLSVTDTG SGSQRPRPRV LLKAPTLAEM
EEMNTSEEEE SPCGEVALKR DRSFSEHDLA QLRSEMASGL QSAAQPPGGT EPPRARAGSM
HSWRPSSRDQ GFCPVSGQSQ PLPSSALPSS LSSVDGPEAA SPDTRHLWLE FSHPVESLAL
TVEEVVDVRR VLVKAEMERF LQDKELFSSL KRGKICCCCR AKFPLFSWPP TCLFCKRAVC
TSCSVKMKMP SKKYGHIPVY TLGFESLQRV PTTKATPTLR RDAFQSLQGP KWRSVEEEFP
HIYAHGCVLK DVCSDCTSFV ADVVCSSRKS VDVLNATPRR SRQTQSLYIP NTRTLNFQ
