SPIR2_DANRE
ID SPIR2_DANRE Reviewed; 606 AA.
AC Q5U3H9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein spire homolog 2;
DE Short=Spir-2;
GN Name=spire2; ORFNames=zgc:103506;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) 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 (By similarity). Also acts in the nucleus: together with SPIRE1
CC and SPIRE2, promotes assembly of nuclear actin filaments in response to
CC DNA damage in order to facilitate movement of chromatin and repair
CC factors after DNA damage (By similarity).
CC {ECO:0000250|UniProtKB:Q8K1S6, ECO:0000250|UniProtKB:Q8WWL2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8K1S6}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8K1S6}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8K1S6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8K1S6}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8K1S6}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8K1S6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8K1S6}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8K1S6}.
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; BC085537; AAH85537.1; -; mRNA.
DR AlphaFoldDB; Q5U3H9; -.
DR SMR; Q5U3H9; -.
DR STRING; 7955.ENSDARP00000031129; -.
DR PaxDb; Q5U3H9; -.
DR ZFIN; ZDB-GENE-041114-29; spire2.
DR eggNOG; ENOG502QQPN; Eukaryota.
DR InParanoid; Q5U3H9; -.
DR PhylomeDB; Q5U3H9; -.
DR PRO; PR:Q5U3H9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
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: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; IBA:GO_Central.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IBA:GO_Central.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; ISS:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IBA:GO_Central.
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 InterPro; IPR011019; KIND_dom.
DR InterPro; IPR029901; Spire.
DR InterPro; IPR029904; Spire2.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR21345; PTHR21345; 1.
DR PANTHER; PTHR21345:SF5; PTHR21345:SF5; 1.
DR Pfam; PF16474; KIND; 1.
DR SMART; SM00750; KIND; 1.
DR SMART; SM00246; WH2; 4.
DR PROSITE; PS51377; KIND; 1.
DR PROSITE; PS51082; WH2; 2.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..606
FT /note="Protein spire homolog 2"
FT /id="PRO_0000320025"
FT DOMAIN 21..219
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 263..277
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 357..374
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 147..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..574
FT /note="Spir-box"
FT COMPBIAS 160..175
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 68134 MW; 31AFA76097912140 CRC64;
MARSADRSAE DGDSRAGIRE LSLEEVLKSY EQPINEEQAW AVCFQCCGDL RAPRPQPHPR
RPELQIRDPA SIILHRDGRV TALLQSCDDS NAGCESAADG KLVQSLGVAI YRALDWGLDD
SEERELSPQL EQLIEFMVGG PDCGQSKHCG SNAAKDEGYS GQDEEEEEEE EEEEEGAGRG
IHTVQQVMTM CASRLANPVL APEHYQAVCR ALFLETLELQ TFLSRIRDAK EMLKKIRKEE
PQEDSAAELD ALQHTDWARL WVQLMKELRQ GVKLKKVEEQ PFNPLPTEFS LTPFEMLMQD
IRLRKYKLRK VVVDGNIPTC VKRNAHELIL DFIRSRPPLK PVSERSLPPP PQRPQSLHDR
VLAEIRQDHK LRPVELPSSK RSFGSLPCLA HTCQCDIKST SCIDLSVTGA GSRPSSRIRV
LLKAPTLAEM EEMNIFEDED SPDGVDMRRV ESSPTPLKRD RSFSEHDLDE LRGEMMSDSP
QHSGVAALRA ERPRSHTLTG VYQASFPGFE RRSASTCRSL SSDDRSSDPG GDSASHGLSR
HQWMEEFCHP VETLALTVDG VINVRRILVK AEMEKYMQNK ELFSNLKKGK VCVSLSYMID
ISPTAQ
