KIF1B_RAT
ID KIF1B_RAT Reviewed; 1816 AA.
AC O88658; Q65Z71; Q8R524;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Kinesin-like protein KIF1B;
GN Name=Kif1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9808286; DOI=10.1016/s0171-9335(98)80099-x;
RA Faire K., Gruber D., Bulinski J.C.;
RT "Identification of kinesin-like molecules in myogenic cells.";
RL Eur. J. Cell Biol. 77:27-34(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CHP1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12204119; DOI=10.1093/oxfordjournals.jbchem.a003246;
RA Nakamura N., Miyake Y., Matsushita M., Tanaka S., Inoue H., Kanazawa H.;
RT "KIF1Bbeta2, capable of interacting with CHP, is localized to synaptic
RT vesicles.";
RL J. Biochem. 132:483-491(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX PubMed=15086790; DOI=10.1111/j.1600-0854.2003.00165.x;
RA Matsushita M., Tanaka S., Nakamura N., Inoue H., Kanazawa H.;
RT "A novel kinesin-like protein, KIF1Bbeta3 is involved in the movement of
RT lysosomes to the cell periphery in non-neuronal cells.";
RL Traffic 5:140-151(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1057; SER-1454; SER-1487 AND
RP SER-1613, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Motor for anterograde transport of mitochondria. Has a
CC microtubule plus end-directed motility (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Isoform 1]: Mediates the transport of synaptic vesicles in
CC neuronal cells. {ECO:0000269|PubMed:12204119}.
CC -!- FUNCTION: [Isoform 2]: Involved in the translocation of lysosomes from
CC perinuclear regions to the cell periphery.
CC {ECO:0000269|PubMed:15086790}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with KIFBP (By similarity).
CC Interacts (via C-terminus end of the kinesin-motor domain) with CHP1;
CC the interaction occurs in a calcium-dependent manner (PubMed:12204119).
CC Interacts with MADD (via death domain) (By similarity).
CC {ECO:0000250|UniProtKB:O60333, ECO:0000250|UniProtKB:Q60575,
CC ECO:0000269|PubMed:12204119}.
CC -!- INTERACTION:
CC O88658-1; P61023: Chp1; NbExp=4; IntAct=EBI-6143515, EBI-917838;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Mitochondrion {ECO:0000250|UniProtKB:O60333}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q60575}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle {ECO:0000269|PubMed:12204119}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=KIF1Bbeta2;
CC IsoId=O88658-1; Sequence=Displayed;
CC Name=2; Synonyms=KIF1Bbeta3;
CC IsoId=O88658-2; Sequence=VSP_016617, VSP_016619, VSP_016622;
CC Name=3; Synonyms=KIF1B;
CC IsoId=O88658-3; Sequence=VSP_016617, VSP_016618, VSP_016620,
CC VSP_016621;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in the brain with lower
CC expression in testis and liver (at protein level). Isoform 1 is
CC strongly expressed in the brain and ovary, with lower expression in
CC lung, kidney, uterus, testis and liver. Isoform 2 is expressed in non-
CC neuronal cells. {ECO:0000269|PubMed:12204119}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AF083331; AAC33292.1; -; mRNA.
DR EMBL; AB070355; BAB86917.1; -; mRNA.
DR EMBL; AB120429; BAD51401.1; -; mRNA.
DR RefSeq; NP_476548.1; NM_057200.2. [O88658-1]
DR AlphaFoldDB; O88658; -.
DR SMR; O88658; -.
DR CORUM; O88658; -.
DR IntAct; O88658; 5.
DR MINT; O88658; -.
DR STRING; 10116.ENSRNOP00000049243; -.
DR iPTMnet; O88658; -.
DR PhosphoSitePlus; O88658; -.
DR jPOST; O88658; -.
DR PaxDb; O88658; -.
DR PRIDE; O88658; -.
DR Ensembl; ENSRNOT00000087739; ENSRNOP00000074322; ENSRNOG00000057626. [O88658-1]
DR GeneID; 117548; -.
DR KEGG; rno:117548; -.
DR UCSC; RGD:621520; rat. [O88658-1]
DR CTD; 23095; -.
DR RGD; 621520; Kif1b.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000157445; -.
DR InParanoid; O88658; -.
DR OMA; GSMDQKT; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; O88658; -.
DR TreeFam; TF105221; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:O88658; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000057626; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; O88658; baseline and differential.
DR Genevisible; O88658; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IDA:RGD.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; IGI:ARUK-UCL.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; IMP:RGD.
DR GO; GO:0007018; P:microtubule-based movement; ISS:UniProtKB.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; ISO:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISS:UniProtKB.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:1990778; P:protein localization to cell periphery; IMP:RGD.
DR GO; GO:1904647; P:response to rotenone; IEP:RGD.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; IGI:ARUK-UCL.
DR GO; GO:0010970; P:transport along microtubule; IDA:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PTHR24115; PTHR24115; 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; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Microtubule;
KW Mitochondrion; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT CHAIN 2..1816
FT /note="Kinesin-like protein KIF1B"
FT /id="PRO_0000125409"
FT DOMAIN 5..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 556..612
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 1701..1799
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 270..350
FT /note="Interaction with KBP"
FT /evidence="ECO:0000250"
FT REGION 431..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1620..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 470..512
FT /evidence="ECO:0000255"
FT COILED 672..731
FT /evidence="ECO:0000255"
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:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 647
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60575"
FT MOD_RES 652
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60575"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60333"
FT MOD_RES 1613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 289..294
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15086790,
FT ECO:0000303|PubMed:9808286"
FT /id="VSP_016617"
FT VAR_SEQ 342
FT /note="L -> LST (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9808286"
FT /id="VSP_016618"
FT VAR_SEQ 394..434
FT /note="IDPLMDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTA -> T (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15086790"
FT /id="VSP_016619"
FT VAR_SEQ 394..408
FT /note="IDPLMDDYSGSGGKY -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9808286"
FT /id="VSP_016620"
FT VAR_SEQ 707..1816
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9808286"
FT /id="VSP_016621"
FT VAR_SEQ 889..971
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15086790"
FT /id="VSP_016622"
FT CONFLICT 121..122
FT /note="QL -> TC (in Ref. 1; AAC33292)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..144
FT /note="EV -> S (in Ref. 1; AAC33292)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="S -> T (in Ref. 1; AAC33292)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="A -> R (in Ref. 1; AAC33292)"
FT /evidence="ECO:0000305"
FT CONFLICT 533..534
FT /note="HL -> QV (in Ref. 1; AAC33292)"
FT /evidence="ECO:0000305"
FT CONFLICT 557..558
FT /note="RV -> KGF (in Ref. 1; AAC33292)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="H -> HT (in Ref. 1; AAC33292)"
FT /evidence="ECO:0000305"
FT CONFLICT 622..627
FT /note="NRIIMG -> TVSSWV (in Ref. 1; AAC33292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1816 AA; 204170 MW; 7A6EBD08EBAC2BF9 CRC64;
MSGASVKVAV RVRPFNSRET SKESKCIIQM QGNSTSIINP KNPKEAPKSF SFDYSYWSHT
SPEDPCFASQ SRVYNDIGKE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEESQAGIIP
QLCEELFEKI NDNCNEDMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYT DIADLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKKQ DPETNLSTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVDN CTSKSKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIKCNAVI
NEDPNAKLVR ELKEEVTRLK DLLRAQGLGD IIDIDPLMDD YSGSGGKYLK DFQNNKHRYL
LASENQRPGN FSTASMGSLT SSPSSCSLNS QAGLTSVTSI QERIMSTPGG EEAIERLKES
EKIIAELNET WEEKLRKTEA IRMEREALLA EMGVAIREDG GTLGVFSPKK TPHLVNLNED
PLMSECLLYY IKDGITRVGQ ADAERRQDIV LSGAHIKEEH CIFRSERNNT GEVIVTLEPC
ERSETYVNGK RVAHPVQLRS GNRIIMGKNH VFRFNHPEQA RAEREKTPSA ETPSEPVDWT
FAQRELLEKQ GIDMKQEMEK RLQEMEILYK REKEEADLLL EQQRLDYESK LQALQKQVET
RSLAAETTEE EEEEEEVPWT QHEFELAQWA FRKWKSHQFT SLRDLLWGNA VYLKEANAIS
VELKKKVQFQ FVLLTDTLYS PVPPELLPTE MGKTHEDRPF PRTVVAVEVQ DLKNGATHYW
SLDKLKQRLD LMREMYDRAG EVGSNAQDDS ETTMTGSDPF YDRFHWFKLV GSSPIFHGCV
NERLADRTPS PTFSTADSDI TELADEQQDA MEDFDDEAFV DDTGSDAGTE EGSELFSDGH
DPFYDRSPWF ILVGRAFVYL SNLLYPVPLI HRVAIVSEKG EVRGFLRVAV QAIAADEEAP
DYGSGIRQSG TAKISFDNEY FNQSDFPSAA MTRSGLSLEE LRIVEGQGQS SEVISPPEEV
NRMNDLDLKS GTLLDGKMVM EGFSEEIGNH LKLGSAFTFR VTVLQASGIL PEYADIFCQF
NFLHRHDEAF STEPLKNNGR GSPLGFYHVQ NIAVEVTESF VDYIKTKPIV FEVFGHYQQH
PLHLQGQELN SPPQPSRRFF PPPMPLSRPV PATKLNTMNK TSLGQSMSKY DLLVWFEISE
LEPTGEYIPA VVDHTAGLPC QGTFLLHQGI QRRITVTIIH EKGSELHWKD VRELVVGRIR
NKPEVDEAAV DAILSLNIIS AKSLKSSHSS SRTFYRFEAV WDSSLHNSLL LNRVTPYGEK
IYMTLSAYLE LDHCIQPAVI TKDVCMVFYS RDAKISPPRS LRNLFGSGYS KSPDSNRVTG
IYELSLCKMA DTGSPGMQRR RRKVLDTSVA YVRGEENLAG WRPRGDSLIL EHQWELEKLE
LLHEVEKTRH FLLLRERLGD SIPKSMSDSL SPSLSSGTLS TSTSISSQIS TTTFESAITP
SESSGYDSAD IESLVDREKE LATKCLQLLT HTFNREFSQV HGSISDCKLS DISPIGRDPS
VSSFSSSTLT PSSTCPSLVD SRSSSMDQKT PEANSRASSP CQEFEQFQII PTVETPYLAR
AGKNEFLNLV PDIEEVRAGS VVSKKGYLHF KEPLSSNWAK HFVVVRRPYV FIYNSDKDPV
ERGIINLSTA QVEYSEDQQA MLKTPNTFAV CTKHRGVLLQ ALNDKDMNDW LYAFNPLLAG
TIRSKLSRRC PSQPKY
