SPIR1_MACFA
ID SPIR1_MACFA Reviewed; 584 AA.
AC Q4R707;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Protein spire homolog 1;
GN Name=SPIRE1; ORFNames=QtsA-16668;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000312|EMBL:BAE01117.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as an actin nucleation factor, remains associated with
CC the slow-growing pointed end of the new filament. Involved in
CC intracellular vesicle transport along actin fibers, providing a novel
CC link between actin cytoskeleton dynamics and intracellular transport.
CC Required for asymmetric spindle positioning and asymmetric cell
CC division during oocyte meiosis. Required for normal formation of the
CC cleavage furrow and for polar body extrusion during female germ cell
CC meiosis. Also acts in the nucleus: together with FMN2, promotes
CC assembly of nuclear actin filaments in response to DNA damage in order
CC to facilitate movement of chromatin and repair factors after DNA
CC damage. {ECO:0000250|UniProtKB:Q52KF3}.
CC -!- SUBUNIT: Interacts with FMN2. {ECO:0000250|UniProtKB:Q08AE8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q52KF3}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q08AE8}. Cell membrane
CC {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q52KF3}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q52KF3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q52KF3}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q52KF3}. Note=Punctate spots in perinuclear
CC region and cytoplasm, co-localized with Rab11. Detected at the cleavage
CC furrow during asymmetric oocyte division and polar body extrusion.
CC {ECO:0000250|UniProtKB:Q52KF3}.
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; AB169023; BAE01117.1; -; mRNA.
DR AlphaFoldDB; Q4R707; -.
DR SMR; Q4R707; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
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; 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:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; ISS:UniProtKB.
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; ISS:UniProtKB.
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 SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51377; KIND; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..584
FT /note="Protein spire homolog 1"
FT /id="PRO_0000309570"
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 224..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..404
FT /note="Spir-box"
FT COILED 71..99
FT /evidence="ECO:0000255"
FT COMPBIAS 12..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..273
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 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AE8"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AE8"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AE8"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AE8"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AE8"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52KF3"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52KF3"
SQ SEQUENCE 584 AA; 67184 MW; 88374E229EEADDF1 CRC64;
MANTVEADGS NDEGYEAAEE GPEDEEDEKR EISAIRSYRD VMKLCAAHLP TESDAPNHYQ
AVCRALFAET MELHTFLAKV KSAKENLKKI QEMEKSDESS TDLEELKNAD WARFWVQVMR
DLRNGVKLKK VQERQYNPLP IEYQLTPYEM LMDDIRCKRY TLRKVMVNGD IPPRLKKSAH
EIILDFIRSR PPLNPVSARK LKPTPPRPRS LHERILEEIK AERKLRPVSP EEIRRSRLDV
TTPESTKNLM ESSMVNGGLT SQTKENGLSS AEQVPAQRKK LLKAPTLAEL DSSESEEETL
HKSTSSSSVS PSFPEEPVLE AVSTRKKPPK FLPISSTPQP ERRQPPQRRH SIEKETPTNV
RQFLPPSRQS SRSLEEFCYP VECLALTVEE VMHIRQVLVK AELEKYQQYK DIYTALKKGK
LCFCCRTRRF SFFTWSYTCQ FCKRPVCSQC CKKMRLPSKP YSTLPIFSLG PSALQRGESS
MRSEKPSTAH HRPLRSIARF SSKSKSMDKS DEELQFPKEL MEDWSTMEVC VDCKKFISEI
ISSSRRSLVL ANKRARLKRK TQSFYMSPPG PSEYCPSERT ISEI
