ID W5MUY7_LEPOC Unreviewed; 745 AA.
AC W5MUY7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Spire type actin nucleation factor 1 {ECO:0000313|Ensembl:ENSLOCP00000012196.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012196.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012196.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the spire family.
CC {ECO:0000256|ARBA:ARBA00010956}.
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DR EMBL; AHAT01004699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015213485.1; XM_015357999.1.
DR AlphaFoldDB; W5MUY7; -.
DR Ensembl; ENSLOCT00000012217.1; ENSLOCP00000012196.1; ENSLOCG00000009960.1.
DR GeneID; 102688602; -.
DR CTD; 557962; -.
DR GeneTree; ENSGT00390000003058; -.
DR HOGENOM; CLU_018839_0_0_1; -.
DR OrthoDB; 2900844at2759; -.
DR Proteomes; UP000018468; Linkage group LG11.
DR Bgee; ENSLOCG00000009960; Expressed in camera-type eye and 11 other cell types or tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; 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; cd15767; FYVE_SPIR1; 1.
DR CDD; cd22186; WH2_Spire1-2_r3; 1.
DR CDD; cd22078; WH2_Spire1_r2-like; 1.
DR CDD; cd22080; WH2_Spire1_r4; 1.
DR CDD; cd22065; WH2_Spire_1-2_r1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR029905; Spir-1_FYVE-rel_dom.
DR InterPro; IPR029901; Spire.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR21345:SF8; PROTEIN SPIRE HOMOLOG 1; 1.
DR PANTHER; PTHR21345; SPIRE; 1.
DR Pfam; PF16474; KIND; 1.
DR SMART; SM00750; KIND; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51377; KIND; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 41..233
FT /note="KIND"
FT /evidence="ECO:0000259|PROSITE:PS51377"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 84391 MW; 2922FE87DABD82A5 CRC64;
MAERRGADKE GLTAGALRQP GSDEQTSGDV NMEGGDGADE LSLEEILKLY SQPINEEQAW
AVCYQCCRTL AQGFRGSSAG ARVEGRAWRI EGAADVRICK DGAVRLHHRQ GGSGKPTSPC
TASEVIESLG IMIYKALDYG LKANEERELS PTLEQLIDRM TNMAEQEPDG CPDEGYEATE
EEDEAEEDAG TVPSLRGYRD VIKLCSSHLP SSSDAPSHYQ AVCRALYAET KELRTFLEKI
KSAKENLRKM EGAKAEEPTR DLNELQNADW ARFWVQVMRD LRHGVKLKKV QERQYNPLPI
EFQLTPYEML MDDIRSKRYT LRKVMVNGNI PPKLKKSAHE VILDFIRSRP PLNPVAARKL
KPYPQRPRSL HERILEEIKA ERKLRPVSPD EIRRSRLDVS STPEPPRRGG ASALANGKLP
AQSQRNGVGG AQATIQRKRL LKAPTLAELD SSDSEEETTR MSVSSSSMST SQVDDMSPDS
AVGRKTPPKF LPISSTPQPE RRQPPQRRHS IEKETPTNVR QFMPPSRQSS KSLEEFCYPV
ECLALTVEEV MHIRQVLVKA ELEKFQQYKD VYNALKKGKL CFCCRTKRFS LFTWSYTCQF
CKRPVCSQCC KKMRLPSKPY ANLPIYSLGS SALQKEEAIP KPERPSTSHH RHHSLHRTVS
RLSKSERSER SREELELPRE LTEDWSTMEV CVDCKKFISE IISSSKRSLS LATKRARLKR
KTQSFYMSSP NAAEYRPSER TIKEV
//
