ID W5M2E2_LEPOC Unreviewed; 1384 AA.
AC W5M2E2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Kinesin family member 15 {ECO:0000313|Ensembl:ENSLOCP00000002550.1};
GN Name=KIF15 {ECO:0000313|Ensembl:ENSLOCP00000002550.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002550.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002550.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-12 subfamily.
CC {ECO:0000256|ARBA:ARBA00034488}.
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DR EMBL; AHAT01012297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01012298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01012299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000002550; -.
DR Ensembl; ENSLOCT00000002556.1; ENSLOCP00000002550.1; ENSLOCG00000002182.1.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156463; -.
DR HOGENOM; CLU_005295_0_0_1; -.
DR InParanoid; W5M2E2; -.
DR OMA; SEYNFKM; -.
DR Proteomes; UP000018468; Linkage group LG11.
DR Bgee; ENSLOCG00000002182; Expressed in embryo and 10 other cell types or tissues.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01373; KISc_KLP2_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR044986; KIF15/KIN-12.
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; PTHR37739; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR PANTHER; PTHR37739:SF8; KINESIN-LIKE PROTEIN KIN-12D; 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 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:UP000018468}.
FT DOMAIN 34..372
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 406..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..406
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 628..658
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 974..1064
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1289..1370
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 792..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1384 AA; 156356 MW; 7B3CA7AC560DFC13 CRC64;
MGTGIKGDSG DAAHLSCKSP LVSGTYFNSG DGDAIKVFVR VRPLTQGTGL STDGDPSLCL
TVTSPNTIRL HSKPEPRVFT YDHVADMDVS QEAVFSSVGK NIVESCVNGY NGTIFAYGQT
GSGKTFTMLG PAESDNFTHD MRGVIPRSFE YLFFLINREA EKSRNGKSFL CKCSFIEIYN
EQIFDLLDSA SASLFLRENI KKGVFVDGAV EKIITSAGEA YQVLSTGWRN RRVASTSMNR
ESSRSHAVFT VTLESKETVN EIVNIRSSQL NLVDLAGSER QKDTHAEGTR LKEAGSINRS
LSCLGHVIMA LVDVSNGKSR HICYRDSKLT FLLRDSLGGN ARTFIIANVH PGSKCFGETL
STLHFAQRAK LIKNKAVINE DTQGNVRQLQ AEVKKLKEQL AQALAAQTPA GARGGPDHEG
HSVPAENEHK HRFLEAMLLW EKSESEKKNL LQKVTQLEET WAKKEKFIQS NRMILKFRED
HISRLEKSLK ESQGGLSSQE SEAAVSQLKQ EIQILREQVE QHPRVAKYAV ENHSLREENQ
RLRSLEPVKR AQELSAQVAA ELEKAFREAS AAEKLPGVPP LFSTPVAAEN VSSVSVERLR
AQLMQKQAEL TTTVQAYEEY KELTKKRLLE MESEKQYLEK ANQHLENILE ATQAHTRQEV
SQLNKKHFET IKNLTTPTRG YCLRSRLVPH FSPDHSMDLS ARSLPAEDPV DDILNEPVPP
EMNELACEAL TEELETVQEQ VSALQLKLDE EEVKNRKLLQ QIGKLEEHSN KMEELLSSER
SNWSKEQQNL QDHISSLEKD LREEKTRTDX RRGAGGDLEP LRTRESSFKA SRSRLHCSCN
STALLTLFQV TDDGVLFFLI LEDLKLEHEK LLEERRSLQD SHDTLQEVMK YESEEHKQRV
AESQRENAAL QAELSKLLES MKTEKERNSN LTSQLKEDKE TTSKELLRAL DENVDLKKHI
SSLTVQSEQQ TAELHSLKQS LTAANTSVAE LEKKCETEKE FVVDILNQTQ ELRNTLNEKN
EMLAVLSSEL EDIKEKYCAA LAAREESRAL IARHEKEVID LREAMERRVS SDKIEVSGGP
CLLTRKQTSL NGLFFNNLSL KPVAGLELRN EPRDISVVKK KLKQKNELKS PKITSEQNHK
AVLPATPLAQ TQTPKTPSSF STDLTKVLEA QEQELENRRS SIVTLEMLVK EFSAERLAQN
EEILRLKKAQ LCEKENLRLE LTDQCYTLQN QMAQNCGSSV EKDGNSHEAV MKELKEERKA
RVAAMTKLSE LEVDLQRTSA TLSSAETCIQ QMTSELRDRS IELKELREKD LDHEKLAKEV
DVLRKQVDFL AEENGKLVGH QNLNQKIQYL VKLKKENTKL IEDNEKLRLE NFNLKESCKK
IQVS
//
