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Database: UniProt
Entry: A0A2I3MHG0_PAPAN
LinkDB: A0A2I3MHG0_PAPAN
Original site: A0A2I3MHG0_PAPAN 
ID   A0A2I3MHG0_PAPAN        Unreviewed;      1816 AA.
AC   A0A2I3MHG0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Kinesin family member 1B {ECO:0000313|Ensembl:ENSPANP00000035173.1};
GN   Name=KIF1B {ECO:0000313|Ensembl:ENSPANP00000035173.1};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000035173.1, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000035173.1, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000035173.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   Ensembl; ENSPANT00000054162.2; ENSPANP00000035173.1; ENSPANG00000006371.3.
DR   GeneTree; ENSGT00940000157445; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000028761; Chromosome 1.
DR   Bgee; ENSPANG00000006371; Expressed in skeletal muscle tissue and 69 other cell types or tissues.
DR   ExpressionAtlas; A0A2I3MHG0; baseline.
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; 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:UP000028761};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          5..354
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          556..612
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1701..1799
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1550..1570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1618..1660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          675..731
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1550..1568
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   1816 AA;  204587 MW;  BFBBDBA2012DD504 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 CTSKSKKKKK
     TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIKCNAVI
     NEDPNAKLVR ELKEEVTRLK DLLRAQGLGD IIDIDPLIDD YSGSGSKYLK DFQNNKHRYL
     LASENQRPGH FSTASMGSLT SSPSSCSLNS QVGLTSVTSI QERIMSTPGG EEAIERLKES
     EKIIAELNET WEEKLRKTEA IRMEREALLA EMGVAIREDG GTLGVFSPKK TPHLVNLNED
     PLMSECLLYY IKDGITRVGQ ADAERRQDIV LSGAHIKEEH CIFRSERNNS GEVIVTLEPC
     ERSETYVNGK RVSQPVQLRS GNRIIMGKNH VFRFNHPEQA RAEREKTPSA ETPSEPVDWT
     FAQRELLEKQ GIDMKQEMEK RLQEMEILYK KEKEEADLLL EQQRLDYESK LQALQKQVET
     RSLAAETTEE EEEEEEVPWT QHEFELAQWA FRKWKSHQFT SLRDLLWGNA VYLKEANAIS
     VELKKKVQFQ FVLLTDTLYS PLPPELLPTE MEKTHEDRPF PRTVVAVEVQ DLKNGATHYW
     SLEKLKQRLD LMREMYDRAG EMASSAQDES ETTVTGSDPF YDRFHWFKLV GSSPIFHGCV
     NERLADRTPS PTFSTADSDI TELADEQQDE MEDFDDEAFV DDAGSDAGTE EGSDLFSDGH
     DPFYDRSPWF ILVGRAFVYL SNLLYPVPLI HRVAIVSEKG EVRGFLRVAV QAIAADEEAP
     DYGSGIRQSG TAKISFDNEY FNQSDFSSVA MTRSGLSLEE LRIVEGQGQS SEVITPPEEI
     NRMNDLDLKS STLLDGKMVM EGFSEEIGNH LKLGSAFTFR VTVLQASGIL PEYADIFCQF
     NFLHRHDEAF STEPLKNNGR GSPLGFYHVQ NIAVEITESF VDYIKTKPIV FEVFGHYQQH
     PLHLQGQELN SPPQPCRRFF PPPMPLSKPV PATKLNTMSK TSLGQSMSKY DLLVWFEISE
     LEPTGEYIPA VVDHTAGLPC QGTFLLHQGI QRRITVTIIH EKGSELHWKD VRELVVGRIR
     NKPEVDEAAV DAILSLNIIS AKYLKSSHNS SRTFYRFEAV WDSSLHNSLL LNRVTPYGEK
     IYMTLSAYLE LDHCIQPAVI TKDVCMVFYS RDAKISPPRS LRSLFGSGYS KSPDSNRVTG
     IYELSLCKMS DTGSPGMQRR RRKILDTSVA YVRGEENLAG WRPRGDSLIL EHQWELEKLE
     LLHEVEKTRH FLLLRERLGD SIPKSMSDSL SPSLSSGTLS TSTSISSQIS TTTFESAITP
     SESSGYDSAD IESLVDREKE LATKCLQLLT HTFNREFSQV HGSISDCKLS DISPIGRDPS
     ESSFSSATLT PSSTCPSLVD SRSNSLDQKT PEANSRASSP CPEFEQFQIV PAVETPYLAR
     AGKNEFLNLV PDIEEIRPGS VVSKKGYLHF KEPLYSNWAK HFVVVRRPYV FIYNSDKDPV
     ERGIINLSTA QVEYSEDQQA MVKTPNTFAV CTKHRGVLLQ ALNDKDMNDW LYAFNPLLAG
     TIRSKLSRRC PSQPKY
//
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