ID W5KLA5_ASTMX Unreviewed; 2019 AA.
AC W5KLA5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Kinesin family member 26A {ECO:0000313|Ensembl:ENSAMXP00000008367.2};
GN Name=KIF26A {ECO:0000313|Ensembl:ENSAMXP00000008367.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000008367.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000008367.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; ENSAMXT00000008367.2; ENSAMXP00000008367.2; ENSAMXG00000008141.2.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000159075; -.
DR HOGENOM; CLU_002423_0_0_1; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000008141; Expressed in embryo and 13 other cell types or tissues.
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 GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00106; KISc; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 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; PTHR21608:SF6; KINESIN-LIKE PROTEIN KIF26A; 1.
DR PANTHER; PTHR21608; UNCHARACTERIZED; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000018467}.
FT DOMAIN 367..719
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1800..1879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1922..1949
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2019 AA; 217233 MW; 998B060BDC414038 CRC64;
QTSTEEKSEG EEKQRAPQVE GCSSAESSCS PEPSPRKRLN SAEEERRSPR PPPEGAGSER
ELTTKSHLCA HCHIVVAELK RQALALTDPA SLKDPGFATF LLEQLQVLDC TEQGGHEGAR
CQVCATPVQQ LRQQALQALQ EPCHGVEMPA LPASTFSSEQ PTRLTAHSMV TLSSRPPTSR
IPHPANSMLT VAEQRRGLAW TPSSKPSVQV TVGGGPLTGS LGSVTIQAQQ YLEGMWSISR
VNNFLPQPSP TQGPIAESVQ PMPPDTSISA VSLTPPRQRS PVQYGPAAPL SSSQPTSAAA
SFFIRAAQKL NLSSSKRKKT QPPVLLPPEP SIYPTNFSSI IQLSPPPAPP CLLRAGSKAK
ENPGMGKVKV MMRICPSLGV QESSDSMSFL KVDQRKKQLT LYEPSLLAQP TAAHRRTPLA
APKMFAFDAV FTQDASQAEV CSGTVAEVIQ SVVNGADGCI FCFGHVKLGK TYTMIGKDSS
AQSLGIAPCA ISWLFKLISE RKEKTGTRFS VRVSAVEIYG KDESLQDLLS DVSSGSLQDG
QSPGVYLRED PICGTQLQNQ SELRAPTAEK AAHFLDAAIA ARSTSRPDAD EEDRRNSHML
FTLHIYQYRM EKSGKGGMSG GRSRLHLIDL GSCEKVLSKS RDGGGGLCLS LTALGNVILA
LANGAKHVPY RDSKLTMLLR DSLGNINCRT TMIAHVSDSP AHYADSLTTI QLASRIHRVR
KKKSKYASSS SGGESSCDEG RIRRPPHLRP FHPRTVALDP DLPLLLSDPD YSSSSEQSCD
TVIYVGPGGA AISDRELSDN EGPPAFVPII PSLNRKQRGK DGPVDRDHFK CNTFAELQER
LECIDGSEEP SAFVGETIGG QASPKMDITA TKPKEGTGSL SGSPKTSPNK TPSSTLQQDN
VLTKQLSCTT SKLPSSPNHK CKSEHSKWQG TTMSDRDMPE NMCCSRTEGE KDLVSETSSP
CFPVKQVKSS TTQNSEPVVR EKVFFNKKQL PKPAPPPPQQ RDSVRPNGET EEPTATRIPP
IGMSHQTQKQ SGSSISSSHF SRVHHLNPRT PLEVCQLRST LRERCMDRDI LRTTVTLQQP
VELNGEDELV FTLVEELSIG NIVDNGRPSS IISFNSDCSV QAIASGSRPV SIISSINDEF
DAYTSSVGNS ELNIEMVAPL QEETFASLDS RSSSIGSWLS EVSVCTLESD GAQSADVFLP
EGTHIVPGSA FYLDSLGMFH SSPQKQPKNS LNDSGFSFSE LDSDSAASSK LSLSKSSSSP
ESTKTSVRNS PKLTKSNNTN SSPIQTLQGS HDVHCSLPRK MKPTSSPNQS SNISESSNNS
TWRREPLRLE GKPDDPWYRV ENVSDLPVSS NSCSSSKLLK NGISGIPPRK AGTNCNSIPR
IPKMQGPNSS QRVVDGCEKS SCIRKAEVPS KMPQLRRGAT TLGTVPVIHT SIDVKVGLDI
GSSIGSLKFS SLEKYGKANT QDVSMLPKQG GVSPPPPPVR KSSLDQKNRI LLPPSALKSA
YEAAKSSGAR PAKTENEYDA RYRGDSNSLK ASSLKSEHGL LKATSSLKSR GVRGEGGQLY
GSQVSLERCD SLTSLGSKPV LSRENSGASL NGKSSRSIAK FGSPVSTSSP ISTSPPPGVN
LVNVGKNGQV KGSLNARPVP ANGNKARTLS ASNSKALSSS TKSLTASGPR NANLPPSGKS
AIPRSAVGCS SKPTRGTIMG TKQAMRAANS RVSELAASNP PGKQLKGSGD SDSGNDSGVN
LNEDKPTPIP ILPSPYSKIT APRRPQRYSS GHGSDNSSVL SGELPPAMGR TALFYHSGGS
SGYESMIRDS EATGSASSAH DSMSESGMSS SGRTRNSKPP KKRSNGLQRR RLIPAPLPDT
SSLGKKAGAT GQWVDLPPMS GPLKEPFEIK VYEIDDVERL QRRRQEETVE GLMYFNTKLK
DVERRQLQIK ELRVKHETLK EELEDTKARL MMDPSKWMGE FDVDQDLDPE SQEYLEALEQ
ATSELEYCVN LCKSRVMMVT CFDIRVASDI QEGAREVEV
//
