ID SPIR_DROPS Reviewed; 1096 AA.
AC Q29KT5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Protein spire;
GN Name=spir {ECO:0000250|UniProtKB:Q9U1K1}; ORFNames=GA10053;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Acts as an actin nucleation factor, remains associated with
CC the slow-growing pointed end of the new filament. Promotes dissociation
CC of capu from the barbed end of actin filaments. Involved in
CC intracellular vesicle transport along actin fibers, providing a novel
CC link between actin cytoskeleton dynamics and intracellular transport.
CC Required for localization of determinants within the developing oocyte
CC to the posterior pole and to the dorsal anterior corner. Links Rho
CC family signaling and Jnk function to the actin cytoskeleton (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with bsk, Rho1, Rac1, Cdc42 and wash. Interacts with
CC capu (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Note=Punctate spots in perinuclear region and cytoplasm. {ECO:0000250}.
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 -!- PTM: Phosphorylated by Jnk kinase (bsk).
CC {ECO:0000250|UniProtKB:Q9U1K1}.
CC -!- SIMILARITY: Belongs to the spire family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL33089.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH379061; EAL33089.2; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q29KT5; -.
DR SMR; Q29KT5; -.
DR STRING; 46245.Q29KT5; -.
DR eggNOG; ENOG502QQPN; Eukaryota.
DR InParanoid; Q29KT5; -.
DR ChiTaRS; spir; fly.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0022607; P:cellular component assembly; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd15748; FYVE_SPIR; 1.
DR CDD; cd22068; WH2_DmSpire_r3-like; 1.
DR CDD; cd22069; WH2_DmSpire_r4; 1.
DR CDD; cd22078; WH2_Spire1_r2-like; 1.
DR CDD; cd22065; WH2_Spire_1-2_r1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR029901; Spire.
DR InterPro; IPR003124; WH2_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21345:SF3; PROTEIN SPIRE; 1.
DR PANTHER; PTHR21345; SPIRE; 1.
DR Pfam; PF16474; KIND; 2.
DR SMART; SM00750; KIND; 1.
DR SMART; SM00246; WH2; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51377; KIND; 1.
DR PROSITE; PS51082; WH2; 2.
PE 3: Inferred from homology;
KW Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Developmental protein; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1096
FT /note="Protein spire"
FT /id="PRO_0000309574"
FT DOMAIN 111..366
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 436..454
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 500..517
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..800
FT /note="Spir-box"
FT REGION 874..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 315..340
FT /evidence="ECO:0000255"
FT COMPBIAS 36..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 122835 MW; 34E9E80380F06743 CRC64;
MTEHHMDVQA DATQSASESK AMAAPKGKFS EAEEGFLSTS PDSANGDAQQ AHTHTHIISH
THSKGAAKTQ TQTQNGNGTL GMGLGAPMLP GGSRQLLRQA FYQCSCPEQC VTLNNILDSF
KAPLSEDQAW ALIYQFGSLY YKVAAQAHKS GGDYEADLPS RFELHFHRDG NVHFSGAERL
PELVESQEQE ASQQEQQQKQ PQMDDSATSS VDSNAALDRA FDNNNHEHHH HHHHQHHHPV
DSNAALDRAH HTPLVVSHRK IISEMAEIVY TALDYNLPED EECQMSQELE NLFNFMTADE
TDEDCIDEGI DEGDKRWDDE AEEERNDTKE LEHIIETCRN HLQKPALADN HYKAVCRALA
TETIELRVFL QQVLNNGAEK LIKAAESSPT TQKELAKLGF NDWARFWVQV IDELRRGVRL
KKSNFERTPI EYELTPYEIL MGDIRAKKYQ LRKVMVNGDI PPRVKKDAHA MILEFIRSRP
PLKKASERQL GPPRMCTPTP REQLMESIRQ GKELKQITPP EAPPLRQRML PSANSTLSRS
RQRLIKVDFS QLQDDELFFD DSSMSSSHST AATHQHHQQH QPHHAHLAEL HRCSQPKMPP
YPFGGYMVPS QARQECQATA TQLRPRRTMD TSAPRQTLPQ PQAQARPPPP AEPSFTEDEY
HRFFDNALES YDLATQCESR RASLRRHTIV GCQSNLEETH SMPPTRPESR QSDDAGSQSQ
SGASSEAPGI RKSPLMEGDH SQTTDGPPRL DEAHSTSSLG PWNKSFMDKQ TWMERGDDRL
SVTLAEIVHI RSVMTKAELE GLPMDVRVKE DVEKRRVCFL CLRTRFSFFG PWGIQCKLCQ
RTVCAKCYTK MRIPSEHFRN VPLVLISPSL LSSPASSSTP SPSHHAHQAH SSSTGNIMDD
QFPKSLIERL LRSESDRKTR STVGSAPSSP KHQRSNMSTP GISVGPGAGA STSAAPGHAV
EALHDQAAMS ASYSSAMRPS GVMQHHQKHH YNNAMSRSME GPRSLPVHSP AYRPLSNSST
LERKSRFSRG FALFSSGSHL AQTQDQKENL RGEQVPVCND CQGLVNEITS SVKQKRSSAR
NRTIQNLTLD LTPVWK
//
