ID KI26L_CAEEL Reviewed; 1066 AA. AC Q21441; Q9TVW0; Q9U541; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 3. DT 25-MAY-2022, entry version 148. DE RecName: Full=Kinesin-like protein vab-8; DE AltName: Full=Variable abnormal morphology protein 8; GN Name=vab-8; ORFNames=K12F2.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RC STRAIN=Bristol N2; RA Hung M.-S., Way J.; RT "The Caenorhabditis elegans vab-8 gene encodes two kinesin-related proteins RT necessary for axon outgrowth and cell migration."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [3] RP FUNCTION. RX PubMed=8625818; DOI=10.1242/dev.122.2.671; RA Wightman B., Clark S.G., Taskar A.M., Forrester W.C., Maricq A.V., RA Bargmann C.I., Garriga G.; RT "The C. elegans gene vab-8 guides posteriorly directed axon outgrowth and RT cell migration."; RL Development 122:671-682(1996). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9581759; DOI=10.1016/s0896-6273(00)81006-5; RA Wolf F.W., Hung M.-S., Wightman B., Way J., Garriga G.; RT "vab-8 is a key regulator of posteriorly directed migrations in C. elegans RT and encodes a novel protein with kinesin motor similarity."; RL Neuron 20:655-666(1998). RN [5] RP FUNCTION, AND INTERACTION WITH UNC-51. RX PubMed=15539493; DOI=10.1242/dev.01457; RA Lai T., Garriga G.; RT "The conserved kinase UNC-51 acts with VAB-8 and UNC-14 to regulate axon RT outgrowth in C. elegans."; RL Development 131:5991-6000(2004). RN [6] RP FUNCTION. RX PubMed=17237777; DOI=10.1038/nn1835; RA Levy-Strumpf N., Culotti J.G.; RT "VAB-8, UNC-73 and MIG-2 regulate axon polarity and cell migration RT functions of UNC-40 in C. elegans."; RL Nat. Neurosci. 10:161-168(2007). RN [7] RP FUNCTION, AND INTERACTION WITH UNC-73. RX PubMed=17237778; DOI=10.1038/nn1834; RA Watari-Goshima N., Ogura K., Wolf F.W., Goshima Y., Garriga G.; RT "C. elegans VAB-8 and UNC-73 regulate the SAX-3 receptor to direct cell and RT growth-cone migrations."; RL Nat. Neurosci. 10:169-176(2007). RN [8] RP FUNCTION (ISOFORM A), AND INTERACTION WITH UNC-33. RX PubMed=27015090; DOI=10.1371/journal.pgen.1005948; RA Meng L., Chen C.H., Yan D.; RT "Regulation of Gap Junction Dynamics by UNC-44/ankyrin and UNC-33/CRMP RT through VAB-8 in C. elegans Neurons."; RL PLoS Genet. 12:E1005948-E1005948(2016). CC -!- FUNCTION: Required for posterior migration of cells and axon growth CC cones during nervous system assembly. {ECO:0000269|PubMed:15539493, CC ECO:0000269|PubMed:17237777, ECO:0000269|PubMed:8625818}. CC -!- FUNCTION: [Isoform a]: Required for posterior migration of the axon CC growth cone and the ALM cell body (PubMed:9581759, PubMed:17237778). CC May enhance posterior migration by regulating the subcellular location CC or stability of guidance cue receptors such as sax-3 and unc-40, CC promoting their localization to the cell surface (PubMed:17237778). In CC PLM neuron, regulates innexin unc-9 gap junction turnover by CC suppressing unc-9 transport out of the gap junctions (PubMed:27015090). CC {ECO:0000269|PubMed:17237778, ECO:0000269|PubMed:27015090, CC ECO:0000269|PubMed:9581759}. CC -!- FUNCTION: [Isoform b]: Specifically required for CAN cell migration. CC {ECO:0000269|PubMed:9581759}. CC -!- SUBUNIT: Interacts with unc-51 and unc-73 (PubMed:15539493, CC PubMed:17237778). Isoform a: Interacts with unc-33 isoform c CC (PubMed:27015090). {ECO:0000269|PubMed:15539493, CC ECO:0000269|PubMed:17237778, ECO:0000269|PubMed:27015090}. CC -!- INTERACTION: CC Q21441; Q23023: unc-51; NbExp=4; IntAct=EBI-2412191, EBI-329049; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:9581759}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; Synonyms=vab-8l; CC IsoId=Q21441-1; Sequence=Displayed; CC Name=b; Synonyms=vab-8s; CC IsoId=Q21441-2; Sequence=VSP_028697, VSP_028698; CC -!- TISSUE SPECIFICITY: Isoform a is expressed in the AVKR neuron. Isoform CC b is expressed in the CAN cells and in the body wall muscle. Also CC expressed in the motor neurons of the ventral nerve cord and additional CC neurons in the pharynx and head. {ECO:0000269|PubMed:9581759}. CC -!- PTM: Phosphorylated by unc-51. 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; AF108229; AAF17300.1; -; Genomic_DNA. DR EMBL; AF108229; AAF17301.1; -; Genomic_DNA. DR EMBL; BX284605; CAB01577.2; -; Genomic_DNA. DR EMBL; Z78201; CAB01577.2; JOINED; Genomic_DNA. DR EMBL; BX284605; CAB54275.1; -; Genomic_DNA. DR PIR; T23623; T23623. DR PIR; T23624; T23624. DR RefSeq; NP_506063.2; NM_073662.5. [Q21441-1] DR RefSeq; NP_506064.1; NM_073663.3. [Q21441-2] DR AlphaFoldDB; Q21441; -. DR SMR; Q21441; -. DR BioGRID; 44698; 10. DR IntAct; Q21441; 9. DR STRING; 6239.K12F2.2a; -. DR EPD; Q21441; -. DR PaxDb; Q21441; -. DR EnsemblMetazoa; K12F2.2a.1; K12F2.2a.1; WBGene00006874. [Q21441-1] DR EnsemblMetazoa; K12F2.2b.1; K12F2.2b.1; WBGene00006874. [Q21441-2] DR GeneID; 179675; -. DR KEGG; cel:CELE_K12F2.2; -. DR UCSC; K12F2.2a; c. elegans. [Q21441-1] DR CTD; 179675; -. DR WormBase; K12F2.2a; CE31041; WBGene00006874; vab-8. [Q21441-1] DR WormBase; K12F2.2b; CE23870; WBGene00006874; vab-8. [Q21441-2] DR eggNOG; KOG4280; Eukaryota. DR GeneTree; ENSGT00940000163104; -. DR HOGENOM; CLU_287890_0_0_1; -. DR InParanoid; Q21441; -. DR OMA; DNENIAH; -. DR OrthoDB; 1536102at2759; -. DR PRO; PR:Q21441; -. DR Proteomes; UP000001940; Chromosome V. DR Bgee; WBGene00006874; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues. DR ExpressionAtlas; Q21441; baseline and differential. 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; IDA:WormBase. 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; IMP:WormBase. DR GO; GO:0016477; P:cell migration; IMP:WormBase. DR GO; GO:0040011; P:locomotion; IMP:WormBase. DR GO; GO:0008078; P:mesodermal cell migration; IMP:WormBase. DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central. DR GO; GO:1905484; P:negative regulation of motor neuron migration; IMP:UniProtKB. DR GO; GO:0001764; P:neuron migration; IMP:WormBase. DR GO; GO:0018991; P:oviposition; IMP:WormBase. DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase. DR GO; GO:0040025; P:vulval development; IMP:WormBase. 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 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; KW Developmental protein; Differentiation; Microtubule; Motor protein; KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..1066 FT /note="Kinesin-like protein vab-8" FT /id="PRO_0000307306" FT DOMAIN 15..326 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT REGION 328..367 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 332..514 FT /note="Interaction with unc-51" FT REGION 387..411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 402..874 FT /note="Interaction with unc-73" FT REGION 471..491 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 514..715 FT /note="Interaction with unc-51" FT REGION 569..592 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 784..815 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 827..957 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 717..765 FT /evidence="ECO:0000255" FT COILED 987..1021 FT /evidence="ECO:0000255" FT COMPBIAS 333..362 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 798..815 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 863..891 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 894..957 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..484 FT /note="Missing (in isoform b)" FT /evidence="ECO:0000305" FT /id="VSP_028697" FT VAR_SEQ 485..513 FT /note="FGGKTSEKREDFGIMIAQPSIPLMKAKSK -> MPQTSALFEIRRSQITFME FT YFKYTWQRLM (in isoform b)" FT /evidence="ECO:0000305" FT /id="VSP_028698" SQ SEQUENCE 1066 AA; 118211 MW; A848740A95EC6EF0 CRC64; MEACSSKTSL LLHSPLRTIP KLRLCASISS EDVAHGRCSL TDQHLQIEGK NYSKTTFDHI FRTDATQDDM YTAFLSDTIN SVFAGNDATV LAMGAKTNGK DERLYGNSVS RNGLVQMAIT QLMNALDDNK DSEERIQVRM SAIMVSQNES SIVDLLSPFN PDPRHRVVKI VDDARTGVFI DNESEIRVET IDQALFYLNT AVDHRMIQDE HTHRTSHVFI SLSLYSYKMG DKMQGGRRRL CFLDMGIGER NSTNGGMTMP ALGSILLAMV QRNKHIPSRD SSVCQLIRCA LSTSRFTTFV FSFGAKSDDN ENIAHLACKI ARTRAKSMVG HGRKSSGTMS TGTMESNSSS CGTTTITPGG TPRTQRRFEL ESGSELSAAE TVIFLGPNSS RTASPASTTM PFTPTSIRPL HRTTRNHSGV EALSKPLSVE TKSSPTHNCH DGCIHSIPPM LRGHTPFLSA SLKLYDELCS PPSSSRASPA PPAAFGGKTS EKREDFGIMI AQPSIPLMKA KSKYNLDDGK MKQIMQWMET SEAPPILFSS PCYENSATSV EELRECVGIL SHPLEDIIEQ EEESMRTSTA TTGGSKKDHP LRILSKQDLN VEPEIKDKQE ENELELVMAA SLSSMRSHDI LAKLEAMRNA QNGNSVQNIG NSQSNTDMDV SEMDVYRRAS HLEEYAMQRV REIEENKLKN KKKIKLGLNC CQQQSMISSG STVVDWSQIE RKKEKEREVH EEEMRKEMLR ERRAKLKITE LEIKRERNLI DKELDDKKGI ANSIARQLQH FSLSPCRGGR THRSVSTHRI DPPNASLPST PTMSHKKVIG GSLAKLSASG ASGSTGAPPS PALGYHQSLP RHSKLPTSVN GRRASAERER KSNKASRNSC SKERKISGSK EELQWRSPYA QMTSPKSYGG PGTSSSGRGS SAPGSDFETP VVSTTEKSAN GTIPRSKRQS YSASSGYESA NDYHIYSTTN KKPHILDKKR NEEKLSLVRQ ADEIRHRQWQ LKKELEEAKR AIGQEDDAKM IANSSDQRLN GLSRTTMIDA MLQENRILEK RLVACRNHSM LVTTFI //