SPIR1_DANRE
ID SPIR1_DANRE Reviewed; 761 AA.
AC Q1LYM3; Q08BK5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein spire homolog 1;
GN Name=spire1 {ECO:0000250|UniProtKB:Q08AE8};
GN ORFNames=si:ch211-215i13.7, zgc:153436;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAK11121.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye {ECO:0000312|EMBL:AAI24675.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) 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 -!- 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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1LYM3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1LYM3-2; Sequence=VSP_052597, VSP_052598;
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; AL807244; CAP09404.1; -; Genomic_DNA.
DR EMBL; BX004966; CAP09404.1; JOINED; Genomic_DNA.
DR EMBL; BX004966; CAK11121.1; -; Genomic_DNA.
DR EMBL; AL807244; CAK11121.1; JOINED; Genomic_DNA.
DR EMBL; BC124674; AAI24675.1; -; mRNA.
DR RefSeq; NP_001038312.2; NM_001044847.2.
DR RefSeq; XP_005159679.1; XM_005159622.3. [Q1LYM3-1]
DR AlphaFoldDB; Q1LYM3; -.
DR SMR; Q1LYM3; -.
DR STRING; 7955.ENSDARP00000072529; -.
DR PaxDb; Q1LYM3; -.
DR Ensembl; ENSDART00000078066; ENSDARP00000072529; ENSDARG00000035868. [Q1LYM3-1]
DR GeneID; 557962; -.
DR KEGG; dre:557962; -.
DR CTD; 557962; -.
DR ZFIN; ZDB-GENE-061013-119; spire1a.
DR eggNOG; ENOG502QQPN; Eukaryota.
DR GeneTree; ENSGT00390000003058; -.
DR InParanoid; Q1LYM3; -.
DR OrthoDB; 560461at2759; -.
DR PhylomeDB; Q1LYM3; -.
DR TreeFam; TF326239; -.
DR PRO; PR:Q1LYM3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000035868; Expressed in mature ovarian follicle and 18 other tissues.
DR ExpressionAtlas; Q1LYM3; baseline.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
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:0048471; C:perinuclear region of cytoplasm; 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 Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR029901; Spire.
DR InterPro; IPR029905; Spire1.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/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 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..761
FT /note="Protein spire homolog 1"
FT /id="PRO_0000309572"
FT DOMAIN 36..223
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 295..313
FT /note="WH2 1"
FT /evidence="ECO:0000255"
FT DOMAIN 359..376
FT /note="WH2 2"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..577
FT /note="Spir-box"
FT REGION 630..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..246
FT /evidence="ECO:0000255"
FT COMPBIAS 160..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 388..396
FT /note="AGKSISTPQ -> EFIFPSLLS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_052597"
FT VAR_SEQ 397..761
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_052598"
SQ SEQUENCE 761 AA; 85883 MW; 3D6A55EEBD2DCFA8 CRC64;
MTDGGMLISP SALQDPGDGA RPEDIAMDCT DGEEELCLEE ILTLYSQPIN EEQAWAVCYQ
CCRWLTQKHR RKETGVSPPG RIAGPGDVRI RKDGNVKLYQ PSNPDKHTPP SSSIEIIESL
GIMIYKALDY GLKEHEEREL SPPLEQLIDL MTNMADTETD CPDEGYEATE EEDEGEEENA
EVSNVRGYRD IISLCLSHLP SPSDAPNHYQ AVCRALYAET KELRTFLEKI KSAKENLRKM
EGETEEPVRD LNELQNADWA RFWVQVMRDL RHGVKLKKVQ ERQYNPLAIE YQLTPYEMLM
DDIRSKRYKL RKVMVNGDIP PRLKKSAHEI ILEFIRSRPP LNPVSARKLK PHAPQPPTLH
ERILEEIRSE RKLRPVSPDM IRRSRLGAGK SISTPQDLFR SSDIPDGPRK LAISTLSLAN
GTSPARSPVN GVAGGHSLSQ RKRLLKAPTL AELDSSDSEE EQSTRKSDSS SSISTSLVED
TSPESVMGKK PPPQFLPISS TPQPDKRIAP QRRHSIEKEA PTNIRHFLPP SRQNSKSLAH
ALGSGHAEEF CFPVECLTLT VEEVMHIRQV LVKAELEKFQ QYKDIYNALK KGKLCFSCRS
KKFSLFTWSY TCQFCKRPVC SQCCKKMKLP SKPHASLPIS SLGPSILPKK EPGASSAPTD
KTSSTSSHKK NSLQRSLSRS SKHGDRSSSK DELELPEQFT EDWSTMEVCV DCKKFINDII
SNSRRNLSTK RARLHRRTHS VYSSSTSSSN YKPTERTIKE V
