ID   KI26L_CAEBR             Reviewed;        1069 AA.
AC   Q60LV7; A8Y3Z4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Kinesin-like protein vab-8;
DE   AltName: Full=Variable abnormal morphology protein 8;
GN   Name=vab-8; ORFNames=CBG23411;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Required for posterior migration of cells and axon growth
CC       cones during nervous system assembly (By similarity). In PLM neuron,
CC       regulates innexin unc-9 gap junction turnover by suppressing unc-9
CC       transport out of the gap junctions (By similarity).
CC       {ECO:0000250|UniProtKB:Q21441}.
CC   -!- SUBUNIT: Interacts with unc-51 and unc-73. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- PTM: Phosphorylated by unc-51. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIF26 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE601533; CAP39613.3; -; Genomic_DNA.
DR   AlphaFoldDB; Q60LV7; -.
DR   SMR; Q60LV7; -.
DR   STRING; 6238.CBG23411; -.
DR   EnsemblMetazoa; CBG23411.1; CBG23411.1; WBGene00041774.
DR   WormBase; CBG23411; CBP37578; WBGene00041774; Cbr-vab-8.
DR   eggNOG; KOG4280; Eukaryota.
DR   HOGENOM; CLU_287890_0_0_1; -.
DR   InParanoid; Q60LV7; -.
DR   OMA; DNENIAH; -.
DR   OrthoDB; 1536102at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005865; C:striated muscle thin filament; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IEA:EnsemblMetazoa.
DR   GO; GO:0008078; P:mesodermal cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:1905484; P:negative regulation of motor neuron migration; IEA:EnsemblMetazoa.
DR   GO; GO:0001764; P:neuron migration; IEA:EnsemblMetazoa.
DR   GO; GO:0018991; P:oviposition; IEA:EnsemblMetazoa.
DR   GO; GO:0040025; P:vulval development; IEA:EnsemblMetazoa.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24115; PTHR24115; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Differentiation; Microtubule; Motor protein; Neurogenesis;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1069
FT                   /note="Kinesin-like protein vab-8"
FT                   /id="PRO_0000307305"
FT   DOMAIN          15..325
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          328..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..517
FT                   /note="Interaction with unc-51"
FT                   /evidence="ECO:0000250"
FT   REGION          391..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..877
FT                   /note="Interaction with unc-73"
FT                   /evidence="ECO:0000250"
FT   REGION          517..719
FT                   /note="Interaction with unc-51"
FT                   /evidence="ECO:0000250"
FT   REGION          572..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          719..769
FT                   /evidence="ECO:0000255"
FT   COILED          990..1027
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        333..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..850
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..894
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..960
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1069 AA;  118647 MW;  9090B2A42734DA2F CRC64;
     MEACTSKSSL LLHSPLRTIP KLRLCTTISS EDVAYGRCNL TDQHLQIEGK NYSKNTFDHI
     FRTDATQDDM YSAFLSDMIN SVFAGNDATV LAMGAKANGK DERLYGNSVS RNGLIQMAIT
     QLMNAIDDNK DPEERIQVRM SAIMVSQKDS SIVDLLSPFN DPRHRVVKLV DDARTGVFLD
     NESEIRVETI DQALFYLNTA VDHRLIQDEQ THRTSHVFIS LSLYSYKMGD KMQGGRRRLC
     FLDMGIGERN STNGGMTMPA LGSILLAMVQ RNKHIPSRDS SVCQLIRCAL STSRFTTFLF
     SFGSKNDDNE NIAHLACKIA RTRVKSVMGH GRKPSGTFSS GTMDSNGSSS SFGTTTITPG
     GTPRTQRRFE LESGSELSAA ETVIFLGPSC SRTTSPASTT MPSTPTSIRP LHRTTRNHSG
     VDPVSKPLSV ETKSSPTHNC HDGCIHSIPP MLRGHTPFLS PHLKLYDELC SPPNSSCASP
     VLSAPNAFGG KTAERRDDFG IMIAQPHIPL MKAKSKYNLD DGKMKQIMQW METSEAPPIL
     FSSPCYENSA TSLDELRECV GILSHPLEDI IEQEEESMRT STATTGGSKK DHPLRILSKQ
     DLNIDSEAKD KDETELELVM AASLSSMRSH DILAKLEAMR NAQSGQNGQN GNIGTSQSNT
     DMDVSEMDMY RRASHLEEYA MQRVREIEDN KMKNKKKVKL GLNCCQQQSM ISSGSTVVDW
     SQIERKKERE KDAMEEEKRK EVLRERRAKL KITELEIKRE RNMIDKELDD KKGIANSIAR
     QLQHFSLSPC RGGRTHRSVS THRIDPPNAS LPSTPTMSHK KMIGGSLAKL SASGASGSGP
     PSSPSLGYHQ SLPRHSKLPT AVNGRRSSAE RDRKTSKNSR NASSKERRSS GSKEELQWRS
     PYAQMTSPKT YGGPGTSSSG RGSSAPGSDF ETPVVSATEK TANGTMPRSK RQSYSASSGY
     ESANDYHIYA TTNKKANILE KKRNEEKLFL VRQADEIRHR QWQLKKELEE AKRAIGQEED
     AKMIANSSDQ RLNGLSRTTM VDAMLQENRI LEKRLIACRN HSMLVTTFI