GenomeNet

Database: UniProt
Entry: A0A3B1KIL4_ASTMX
LinkDB: A0A3B1KIL4_ASTMX
Original site: A0A3B1KIL4_ASTMX 
ID   A0A3B1KIL4_ASTMX        Unreviewed;      1582 AA.
AC   A0A3B1KIL4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Kinesin family member 20Bb {ECO:0000313|Ensembl:ENSAMXP00000053696.1};
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:ENSAMXP00000053696.1, 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:ENSAMXP00000053696.1}
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; ENSAMXT00000054879.1; ENSAMXP00000053696.1; ENSAMXG00000007718.2.
DR   GeneTree; ENSGT00940000155989; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000007718; Expressed in embryo and 10 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; cd21786; RBD_KIF20B; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
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   PANTHER; PTHR24115:SF534; KINESIN-LIKE PROTEIN KIF20B; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 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; PS00411; KINESIN_MOTOR_1; 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          44..466
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          509..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1320..1466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1541..1582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          605..636
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          811..880
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          909..1000
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1029..1094
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1202..1250
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        511..544
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1332..1380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1381..1403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1432..1466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1582 AA;  179838 MW;  E027A7B424FD738A CRC64;
     MESSLNYKPE RVGAVTVEDL RKDLFVEFSK IPTTQDSVLL EREHLQVYLR IRPFTSTESD
     FGESQDCISI ESPDTVVLKA PRSSLTARQS EKLGPQIAQR FQFSKVYSPE TTQRQIFDGT
     TKALVKDVLA GQNSLIFTYG VTNAGKTFTF LGPETDVGIL PRSLKVIFNS IEGRIYTQNN
     IKPHRCIDFT RLTKDQQDAE ATIKKNLLRR YKENDLQKSS SSMSNSACST LLEGSSCSDL
     NEDSLCLEED SHVKFSVWVS FCEIYNENIH DLLDFASSSS QRRSVLRLCQ DVKGNTFVKD
     LTWIQVNSAD EAYRVLKIGR KNQSFSSTKL NSVSSRSHSI FSIRILRIED MCVPRVQTIS
     ELSLCDLAGS ERCAKTQNRG ERLKEAGNIN TSLLTLGKCI NALRLNQTQS KFQQHIPFRE
     SKLTHYLQGF FSGRGKACMI VNINQCASMF DETLNVLKFS AVAQKVVVVN PKPVFSAVPR
     KSARDVSIMI NNVDKKEWTR RSTLIGWESS LEDVQEDEDD EDMEEGEEDE EEEEQEASDD
     ESVMENTVLE AEDDQELNEL QQKICELKEK LSKADSEKLV MESRIREEVT AEFMELFSNM
     EKDYNERLQR EKEIAEERAE RRLEILKNLV NKNASELADT SIAGDATEET KNEGLDGMIE
     SMQSDLAKIR KDAVAAQTCL EKGAHSPGAV SKLRTQLDQT AKELLKSKQL LEVKTMEIEA
     VRVQFRNSSD QLLEANKNYE SQKIRCAELI TICQEKDDDI SKLQTTLDQN IETANEDRAF
     IETIKEEILH YRNNCKCILS SGNQDVKDQE IQQLEKALQE KDLCLDELKQ KQHSLEQNLK
     DLTDDLAKQT CAHEAAVSLL EAEKAAAVKL ANENRDLASK LCVLQQAASD LSSELRAKQA
     ELSSQASVAA KLSEELQTAR ALIREREEEC SDLFDTVESL KLEAENLRQE LSNQGRKSGC
     EFQETIEALR KECELVMSNT QEKSKRIKTL EQELTQTKEE MCHMQNQCTQ LKQEQDAQKE
     ENQNILGHYE AEKLAVEQMK IRQSELQAEL DDVKQQLAQQ EQHEQAYARS SLRVMELETE
     LSEREGHCAA LQERLLHTQD ELGKAKNVLK KERSRSSSEE QEKTNAESSK ARDEAERRRR
     EMEEQLVHKD AELEAKTQEL LKSKEQVNDG LDQIKSLTLD LQHKEKHISD LHIQHSEGGA
     EAERLRNEIT SLTEEIRKLQ QQLGDLTEER DQALRNLANK KQDIEELKTE QAITASTHEN
     LQQYQETCQA LLAKEKLIAE MRLTLSDKER MQTEQEQVLE ARLNEIESLS EELMMLKEKC
     QKGGETDSTS GNQRQEEQKG EGTARRLTTD EEELERGLGG ELKPNDAPQR PEEKANHVMD
     QSQDKITCKG QLEETAAQDS SVLSTDSERE DKRFPKPQLE ISFTPLKPDR VNVRRPGAEE
     SVTVKIRRTA RKRKSAEMEK SVDSENRKNL RLRGNSRVNI QSVESPTVFS KKANRLKQQD
     SPASLKGRKD GTLQKIGDFI QSSPTLLGSK AKKIMAMVAV KSPESQIAET NNNKPKRSKR
     KLFKTQISSP FDIPSHPVSK DL
//
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