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Database: UniProt
Entry: A0A2K6A9W8_MANLE
LinkDB: A0A2K6A9W8_MANLE
Original site: A0A2K6A9W8_MANLE 
ID   A0A2K6A9W8_MANLE        Unreviewed;      1799 AA.
AC   A0A2K6A9W8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Kinesin family member 1B {ECO:0000313|Ensembl:ENSMLEP00000036842.1};
GN   Name=KIF1B {ECO:0000313|Ensembl:ENSMLEP00000036842.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000036842.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000036842.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   Ensembl; ENSMLET00000060447.1; ENSMLEP00000036842.1; ENSMLEG00000041753.1.
DR   GeneTree; ENSGT00940000157445; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
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   CDD; cd22727; FHA_KIF1B; 1.
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; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   PANTHER; PTHR47117:SF1; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000233140}.
FT   DOMAIN          5..355
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          531..587
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1622..1720
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1471..1492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1539..1581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          650..706
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1471..1491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1799 AA;  202247 MW;  5C18BF498EAE8DCB CRC64;
     MSGASVKVAV RVRPFNSRET SKESKCIIQM QGNSTSIINP KNPKEAPKSF SFDYSYWSHT
     SPEDPCFASQ NRVYNDIGKE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEESQAGIIP
     QLCEELFEKI NDNCNEEMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
     LSKLAVTSYT DIADLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKKH DNETNLSTEK
     VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVDN CTSKVCKKKK
     KTDFIPYRDS VLTWLLRENL GGNSRTAMVA ALSPADINYD ETLSTLRYAD RAKQIKCNAV
     INEDPNAKLV RELKEEVTRL KDLLRAQGLG DIIDIDPLID DYSGSGSKSS MGSLTSSPSS
     CSLNSQVGLT SVTSIQERIM STPGGEEAIE RLKESEKIIA ELNETWEEKL RKTEAIRMER
     EALLAEMGVA IREDGGTLGV FSPKKTPHLV NLNEDPLMSE CLLYYIKDGI TRVGQADAER
     RQDIVLSGAH IKEEHCIFRS ERNNSGEVIV TLEPCERSET YVNGKRVSQP VQLRSGNRII
     MGKNHVFRFN HPEQARAERE KTPSAETPSE PVDWTFAQRE LLEKQGIDMK QEMEKRLQEM
     EILYKKEKEE ADLLLEQQRL DYESKLQALQ KQVETRSLAA ETTEEEEEEE EVPWTQHEFE
     LAQWAFRKWK SHQFTSLRDL LWGNAVYLKE ANAISVELKK KVQFQFVLLT DTLYSPLTPE
     LLPTEMEKTH EDRPFPRTVV AVEVQDLKNG ATHYWSLEKL KQRLDLMREM YDRAGEMASS
     AQDESETTVT GSDPFYDRFH WFKLVGSSPI FHGCVNERLA DRTPSPTFST ADSDITELAD
     EQQDEMEDFD DEAFVDDAGS DAGTEEGSDL FSDGHDPFYD RSPWFILVGR AFVYLSNLLY
     PVPLIHRVAI VSEKGEVRGF LRVAVQAIAA DEEAPDYGSG IRQSGTAKIS FDNEYFNQSD
     FSSVAMTRSG LSLEELRIVE GQGQSSEVIT PPEEINRMND LDLKSSTLLD GKMVMEGFSE
     EIGNHLKLGS AFTFRVTVLQ ASGILPEYAD IFCQFNFLHR HDEAFSTEPL KNNGRGSPLG
     FYHVQNIAVE ITESFVDYIK TKPIVFEVFG HYQQHPLHLQ GQELNSPPQP CRRFFPPPMP
     LSKPETSLGT MAKPHLYKKM YIPAVVDHTA GLPCQGTFLL HQGIQRRITV TIIHEKGSEL
     HWKDVRELVV GRIRNKPEVD EAAVDAILSL NIISAKYLKS SHNSSRLRWE DHLSPGTLVT
     VLCLHFISTY PVCFQLDHCI QPAVITKDVC MVFYSRDAKI SPPRSLRSLF GSGYSKSPDS
     RRRKILDTSV AYVRGEENLA GWRPRGDSLI LEHQWELEKL ELLHEVEKTR HFLLLRERLG
     DSIPKSMSDS LSPSLSSGTL STSTSISSQI STTTFESAIT PSESSGYDST DIESLVDREK
     ELATKCLQLL THTFNREFSQ VHGSISDCKL SDISPIGRDP SESSFSSATL TPSSTCPSLV
     DSRSNSLDQK TPEANSRASS PCPEFEQFQI VPAVETPYLA RAGKNEFLNL VPDIEEIRPG
     SVVSKKGYLH FKEPLYSNWA KHFVVVRRPY VFIYNSDKDP VERGIINLST AQVEYSEDQQ
     AMVKTPNTFA VCTKHRGVLL QALNDKDMND WLYAFNPLLA GTIRPGHLAS ETIREDKSVS
     FSCQQVFQDK RGKGKPPETS VALPVVLGLF YTILYFPCSD LSVAPSLRHS GKYLLAPTW
//
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