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Database: UniProt
Entry: H2TUA3_TAKRU
LinkDB: H2TUA3_TAKRU
Original site: H2TUA3_TAKRU 
ID   H2TUA3_TAKRU            Unreviewed;      1789 AA.
AC   H2TUA3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Kinesin family member 1B {ECO:0000313|Ensembl:ENSTRUP00000028262.3};
GN   Name=kif1b {ECO:0000313|Ensembl:ENSTRUP00000028262.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000028262.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000028262.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000028262.3}
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; 31033.ENSTRUP00000073888; -.
DR   Ensembl; ENSTRUT00000028374.3; ENSTRUP00000028262.3; ENSTRUG00000011194.3.
DR   GeneTree; ENSGT00940000157445; -.
DR   HOGENOM; CLU_001485_10_2_1; -.
DR   Proteomes; UP000005226; Chromosome 3.
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; 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; 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:UP000005226};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          5..355
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1674..1772
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1491..1541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1593..1634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          636..678
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1789 AA;  201283 MW;  5F3043433AF2DD35 CRC64;
     MSGASVKVAV RVRPFNSREM NMDAKCIIHM QGNSTTIANP KAPKEPAKNF SFDYSYWSHT
     TTEDPNFASQ NRVYNDIGKE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEEGQEGIIP
     MLCEDLFEKI NGETNKEGLS YSVEVSYMEI YCERVRDLLN PKNKGNLRVR EHPLMGPYVE
     DLSKLAVTSY TDIADLMDAG NKARTVAATN MNETSSRSHA VFTIVFTQKK HDSETDLSTE
     KVSKISLVDL AGSERADSTG AKGTRLKEGA NINKSLTTLG KVISALAEVD NSTNKSKKKK
     KTDFIPYRDS VLTWLLRENL GGNSRTAMVA ALSPADVNYD ETLSTLRYAD RAKNIKCNAV
     INEDPNNKLV RDLKDEVSRL KELLRAQGLG DILDTPLGSL TASPSSGSLS SQVGLQSVTS
     IQERIMSTPG GEEAIERLKE SEKIIAELNE TWEEKLRKTE AIRMEREALL AEMGVAIRED
     GGTLGVFSPK KTPHLVNLNE DPLMSECLLY YIKDGITRVG QADAERRQDI VLSGAHIREE
     HCIFRSERNA NGDVVVLLVP CEGSETYVNG KRVEDAIQLR SGNRIIMGKN HVFRFNHPEQ
     ARAEREKTPS AETPMEPVDW TFAQRELLEK QGIDMKQEME KRLTEMEILY KKEKEEADQL
     LEQQRLVYES KLQELQKQVE TISLVAETPD EEELYEEEKE EEPKQLSFPW TLHEFELAQW
     AFRKWRYHQF TSLRDQLWGN AVYLKEANAI SVELKKKVQF QFVLLTETLY SPLPPELASQ
     EPEKERDSRP FPRTVVAVEV QDLKNGATHH WSLDKLKQRL EKMREMYDRA GEMASTNQEE
     GEGPLTGNDP FYDRFHWFKL VGSSPIFHGC VNEHLADRTP SPTFSTTDSE ITEMADERQS
     EMSDLIDDEA FVDDTSSDAG TEEGSDIFSD GQDPFYDRSP WFILVGRAFV YLSNLLYSVP
     LVHRVAIVTE KGEVRGFLRV GVQAIAADEE APDYGSGVRQ SGTAKISFDD EYFKKNEFPS
     TVMTRSGMSL EELRIVEGQG QSSEVITPSE ELNRINDIDL KLGNIADTKL SRDGLAGQLE
     VGSIFTFRVT VLQASGVQPE YADIFCQFNF LHRHDEAFST EPLKNSGKGA PLGFYHVQNI
     SVEVTESFIE YIKSKPIVFE VFGHYQQHPL HLHGQELISP PTQSRKYYPI PMPLSKPVPA
     TKLNTITKSN LGQCVSKYDL LVWFEISELE PTGEYIPAIV DHSGGLPCHG TYLLHQGIQR
     RITVTLIHEK GSELHWKDVR ELVVGRIRNK AEVDDSASDG ILSLNIISAK NIKSSHNSNR
     TFYRFEAVWD SSLHNSLLLN RVTPYGEKIY MTLSAYLELD HCIQPAIITK DICMVFYSRD
     AKISPPRSLR NLFVSGYSKT PDCNRVTGIY ELSLCKMSDT GSPGMQRRRR KVLDTSVAYV
     RGEENLAGWR PRGDSLIVEH QWELEKMEQL HEVEKTRHLL LLREKLGDTN PAPSTKSLSE
     LLSPSMSSGT LSTSTSISSQ ISSTTYESAI TPSESSGYDS TDIESLVDRE KELATKCLRL
     LTHTFNSEYN QVVNSISDCK LSDISALGRD PSVTSLSSAT LTPSSTCPSL ADSRCGSIDQ
     KTPENNSRAS SPSYSDYENF PMVPSVETSY LARAGKNEFL NLVPDIEEMR PGSVVSKKGF
     LSFMEPRSNS WVKHFVVVRR PYVFIYNSDK DPVERGVLNL STAQVEYSED QQAMLKTPNT
     FAVCTKHRGI LLQALNEKDM NDWLYAFNPL LAGTIRSKLA RRRSGLTKN
//
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