ID A0A2K5KR43_CERAT Unreviewed; 1388 AA.
AC A0A2K5KR43;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Kinesin family member 15 {ECO:0000313|Ensembl:ENSCATP00000003165.1};
GN Name=KIF15 {ECO:0000313|Ensembl:ENSCATP00000003165.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000003165.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000003165.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSCATT00000014255.1; ENSCATP00000003165.1; ENSCATG00000012043.1.
DR GeneTree; ENSGT00940000156463; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000012043; Expressed in bone marrow and 10 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:UP000233060}.
FT DOMAIN 26..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 370..397
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 581..643
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 712..799
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 846..976
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1086..1131
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1177..1221
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1298..1383
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1388 AA; 160104 MW; 9E82D9B576E652ED CRC64;
MAPGCKTELR SVTNGQSNQT SNEGDAIKVF VRIRPPAERS GSADGEQNLC LSVLSSTSLR
LHSNPEPKTF MFDHVADVDT TQESVFSTVA KSIVESCMSG YNGTIFAYGQ TGSGKTFTMM
GPSESDNFSH NLRGVIPRSF EYLFSLIDRE KEKAGAGKSF LCKCSFIEIY NEQIYDLLDS
ASAGLYLREH IKKGVFVVGA VEQVVTSAAE AYQVLSGGWR NRRVASTSMN RESSRSHAVF
TITIESMEKS NEIVNIRTSL LNLVDLAGSE RQKDTHAEGM RLKEAGNINR SLSCLGQVIT
ALVDVSNGKQ RHVCYRDSKL TFLLRDSLGG NAKTAIIANV HPGSRCFGET LSTLNFAQRA
KLIKNKAVVN EDTQGNVSQL QAEVKRLKEQ LAELVSGQTP PESFLTRDKK KTNYMEYFQE
AMLFFKKSEQ EKKSLIEKVT QLEDLTLKKE KFIQSNKMIV KFREDQITRL EKLHKESRGS
FLPEEQNRLL SELRDEIQTL REQIEHHPRV AKYAMENHSL REENRRLRLL EPVKRAQEMD
AQTIAKLEKA FSEISGIEKS DKNQQGFSPK AQKEPCSFAN TEKLKAQLLQ IQTELNNSKQ
EYEEFKELTR KRQLELESEL QSLQKANLNL ENLLEATKAC KRQEVSQLNK IHAETLKIIT
TPTKVCQLHS RPVPKLSPET GSFGSLYTQN SSILDNDILN EPVPPEMNEQ AFEAISEELS
TMQEQISALQ AKLDEEEHKN LKLQQLVDKL EHHSTQMQEL FSSERIDWTK QQEELLSQLN
VLEKQLQETQ TKNDFLKSEV HDLRVVLHSA DKELSSVKLE YNSFKTSQEK EFNKLSERHM
HVQLQLDNLR LENEKLLESK ACLQDSYDNL QEVMKFEIDQ LSRNLQNCKK ENETLKSDLN
NLMELLEAEK ERNNKLSLQF EEDKENSSKE ILKVLEAVRQ EKQKEMAKCE QQMAKVQKLE
DSLLATEKVI SSLEKSRDSD KKVVADLMNQ IQELRTSVCE KTETIDTLKE ELKDINCKYN
SALVDREESR VLIKKQEVDI LDLKETLRLR ILSEDIERDM LCEDLAHATE QLNMLTEASK
KHSVLLQSAQ EELTKKEALI QELQHKLNQK KEEVEQKKNE YNFKMRQLEH VMDSAAEDPQ
SPKTPPHFQT HLAKLLETQE QEIEDGRASK TSLEHLVTKL NEDREVKNAE ILRMKEQLCE
MENLRLESQQ LREKNWLLQG QLDDIKRQKD NSDQNHPDNQ QLKNEQEESI KERLAKSKIV
EEMLKMKADL EEVQSALYNK EMESLRMTEE VERTRTLESK AFQEKEQLRS KLEEMYEERE
RTSQEMEMLR KQVECLAEEN GKLVGHQNLH QKIQYVVRLK KENVRLAEET EKLRAENVFL
KEKKRSES
//
