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Database: UniProt
Entry: G3NHF4_GASAC
LinkDB: G3NHF4_GASAC
Original site: G3NHF4_GASAC 
ID   G3NHF4_GASAC            Unreviewed;      1689 AA.
AC   G3NHF4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Kinesin family member 1Aa {ECO:0000313|Ensembl:ENSGACP00000004762.1};
GN   Name=KIF1A {ECO:0000313|Ensembl:ENSGACP00000004762.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000004762.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000004762.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000004762.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   STRING; 69293.ENSGACP00000004762; -.
DR   Ensembl; ENSGACT00000004776.1; ENSGACP00000004762.1; ENSGACG00000003623.1.
DR   eggNOG; KOG0245; Eukaryota.
DR   GeneTree; ENSGT00940000156474; -.
DR   InParanoid; G3NHF4; -.
DR   OMA; YEASLCH; -.
DR   TreeFam; TF105221; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000003623; Expressed in telencephalon and 2 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR049780; PH_KIFIA_KIFIB.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          5..355
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          517..573
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1574..1672
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          945..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1524..1555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          431..458
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          629..678
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        954..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1689 AA;  190905 MW;  73F3BFA5C1FDE3ED CRC64;
     MAGASVKVAV RVRPFNSREI GKDSKCIIQM SGNTTTIVNP KQAKDNKSFN FDYSYWSHTS
     PEDINYASQV QVYKDIGEEM LLHAFEGYNV CIFAYGQTGA GKSYTMMGKQ DVKDQQGIIP
     LLCEDLFTKF NDNGDNSMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLMGPYVED
     LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETDNTSEK
     VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVDS GSNKNKKKKK
     VESFIPYRDS VLTWLLRENL GGNSRTAMIA ALSPADINYD ETLSTLRYAD RAKQIRCNAV
     INEDPNNRLV RELKEEVSRL KDLLFSQGLG DIIDMTNAMT GMSPSPSLSA LSSRAGSIAS
     LHDRIMFSPG SEEAIERLKE TEKIIAELNE TWEEKLRRTE AIRMEREALL AEMGVAMRED
     GGTVGVFSPK KTPHLVNLNE DPLMSECLLY YIKDGVTRVG RVDAASRQDI VLSGHFIKDE
     HCTFTSSTDK AREIVVVLEP CEGAETYVNG KRVTEPTVLK SGNRIILGKS HVFRFNHPVQ
     ARAERERTPC AETPAEPVDW AFAQRELLDK QGIDMKQEME QRLQELEDQY RKEREETNNL
     LEQQRLDYES KLEALQKQVD SYYPETLEEE EEPEEEVQWT ERERELAVWS FRKWRCYQFT
     SLRDLLWGNA IFLKEANAIS VELKKKVQFQ FVLLTDTLYS PLPPDLLPPE AAKDREKRHF
     PRTIVAVEVQ DQKNGATHYW TLEKLRQRLD LMREMYDRAA DVPNNTAEDG ENVMTGGDPF
     YDRFPWFRLV GRAFVYLSNL LYPVPLVHRV AIVSERGEVK GFLRVAVQAI SADEEAPDYG
     SGVRQSGTAK ISFEDQQYEK FQSETCSVGL PRSGASQEEL RFVEGEGQNA EPGPSADEVN
     NNTCAAGTDE AESPLKSQGG PLDTTLEHLR VGNVFTFRVT VLQASSIPAE YADIFCQFNF
     IHRHDEAFST EPLKNTGRGP PLGFYHVQNI AVEVTKSFVD YIKSQPIVFE VFGHYQKQPF
     LPLCKDVISP LRPCRRQFPR VMPLSKPDTV PATKLTAMTR PQAGPCHSKH DLMVFFEICE
     LEATGDYIPA VVDHRGGMPC HGTFLLHQQP QGLQRRVTVT IVHESGGDME WKDIRELVVG
     RLRNTPEADE TIIDPNILSL NILSAGYVRP MRDDRQFLDS DMPRTFYRFE AAWDSSMHNS
     LLLNRVTPYG EKIYMTLSAY LEMENCTQPA IITKDVCMVF YSRDTKLSAS RSIRNLFGTG
     SLRAADGNRV TGVYEVSLCN LADAGSPGMQ RRRRRVLDTS VAYVRGEENL AGWRPRSDSL
     ILDHQWELEK LSLLQDVEKT KHYLLLREKL ESTMLMGQES LQSCITEELS ECPQPPEVDQ
     EVPSRSEITT ERQRELAAKC LRLLTHSFNR EYSHVCVSAS ESKISEMSVT MLRDSASISA
     LNTITPSSTC PSLVEGCYGD AELRPPMPRS RAASPAPAPQ QDTEAKKSAG GASETKPRIR
     RFFPDITEIR VSPIVSKKGY LHFLEPNTNG WVKRYVVVRR PYVYIYNAER DSVERAILNL
     SSAQVEYSED QQAMLKTPYT FAVCTEHRGI LLQATNDKEM HDWLYAFNPL LAGTIRSKLS
     RRRAGPMRM
//
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