KI26L_CAEEL
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 03-AUG-2022, entry version 149.
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}.
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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 3 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
