ID G1SED0_RABIT Unreviewed; 1472 AA.
AC G1SED0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Kinesin family member 15 {ECO:0000313|Ensembl:ENSOCUP00000000804.3};
GN Name=KIF15 {ECO:0000313|Ensembl:ENSOCUP00000000804.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000000804.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000000804.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000000804.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000000804.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000000804.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; AAGW02043996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02043997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; G1SED0; -.
DR STRING; 9986.ENSOCUP00000000804; -.
DR PaxDb; 9986-ENSOCUP00000000804; -.
DR Ensembl; ENSOCUT00000000931.4; ENSOCUP00000000804.3; ENSOCUG00000000930.4.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000156463; -.
DR HOGENOM; CLU_005295_0_0_1; -.
DR InParanoid; G1SED0; -.
DR OMA; SEYNFKM; -.
DR TreeFam; TF320478; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000000930; Expressed in testis and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd01373; KISc_KLP2_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR031794; HMMR_C.
DR InterPro; IPR044986; KIF15/KIN-12.
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; PF15908; HMMR_C; 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 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:UP000001811}.
FT DOMAIN 113..450
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..484
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 672..727
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 796..837
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 909..1060
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1089..1130
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1170..1215
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1261..1298
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1382..1467
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1312..1331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 196..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1472 AA; 168436 MW; E0DD114189DD5DB8 CRC64;
MVAVGKHQSP GPTRDGAEAT ARTFDVPQAT PPRRSPAQRA AAELTSTSRP SAKFKPAAIL
SGRYPGALRD WEVGSWAAAS ASRAEGAMAP GCKTELRNVT NCQSNQPSNE GDAIKVFVRL
RPPAEGLRAA EGEQSLCLSV LSATTLRLHS NPEPKTFTFD HVADVDTTQE SVFSAVAKSI
VESCMSGYNG TIFAYGQTGS GKTFTMMGPS ESDNFSHNLR GVIPRSFEYL FSLIDREKEK
AGAGKSFLCK CSFIEIYNEQ IYDLLDSASA GLYLREHIKK GVFVVGAVEQ VVTSAAEAYQ
VLSGGWRNRR VASTSMNRES SRSHAVFTIT VESMEKSNET VNIRTSLLNL VDLAGSERQK
DTHAEGMRLK EAGNINRSLS CLGQVITALV DVGNGKQRHV CYRDSKLTFL LRDSLGGNAK
TAIIANVHPG SRCFGETLST LNFAQRAKLI KNKAVVNEDT QGNVSQLQAE VKRLKEQLAQ
LMSGHMPPGS LLSRDKEKTD YMKYFQEAML FFKKSEQEKK SLVEKITQLE DLTLKKERFI
QSNKMIVKFR EDQITRLEKL HKESRGCFLP EEQDRLLSEL RDEIQTLRDQ IEHHPRVAKY
AMENHSLREE NRRLRLSEPV KRAQEMDAQT IAKLEKVFSE VCGAENNKGQ PGLSPKAQKE
PFANTEKLKS HLLQVQTELN NSKQEYEEFK ELTRKRQLEM ESELQSLQKA NLNLENLLEA
TKACKRQEVS QLNKIHAETL KIITTPTKAY QLRSLLVPKM SPEIGSFTPA HTEESSKVDN
DIANEPIPPE MSEQAFEAIS EELRTVQEQM SSLQVKLDEE EHKNLKLQQH VDRLEHHSTQ
MQELFSSERT DWAKQQQEHL SQLNILDKQL RDTQTKNDFL RSEVHDLRVV LHSADKELSS
VKLEYSAFRA RQEEELSQLS ERHVHVQLQL DSVRLEKEKL LENQACLQDS YENLQEVMKF
EIDQLSKNLQ NCKKENETLK SDLHNLMELL EAEKERNNKL SIKFEEDKEN SSKEILKVLE
AVRQEKQKEM TKCEQQMTKI QKLEESLLTT EKVISSLEKS RDADKEVVAD LMNQIQELRT
SVCEKTETID TLRQELQDIN CKYNSALADR EESKALIKRQ EVDIMDLKET LRLRILSEDI
ERDMLCEDLA HATEQLNMLT EASKKHSGLL QSAQEELSRK EALIQELQHE LNQKKEEVEQ
KKNEYNFKMR QLEHVMDSAA ASPQSPKTPP HFPTHLTKLL ETQEQEMEDE RASKTSLQYL
VSKLTEDREV KNAEILRMKE QLCEMENLRL ESQQLRENTW LLQGQLDAMK RQKDSSGQHP
DHQQLKNEQE EEIIKERLAK SKLVEEMLKM KADLGEVQSA LHSSEADCLR MTAEVERTRT
LEARAFQEKE ELRSKLEEMY EERERALQEM GLLRKQVECL AEENGRLLGH QNLHQKIQYV
VRLKKENVRL LEDIEKLRAE NVFLKEKKKN ES
//
