ID   A0A2K6GGJ7_PROCO        Unreviewed;      1024 AA.
AC   A0A2K6GGJ7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Kinesin family member 5A {ECO:0000313|Ensembl:ENSPCOP00000025365.1};
GN   Name=KIF5A {ECO:0000313|Ensembl:ENSPCOP00000025365.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000025365.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000025365.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A2K6GGJ7; -.
DR   STRING; 379532.ENSPCOP00000025365; -.
DR   Ensembl; ENSPCOT00000036056.1; ENSPCOP00000025365.1; ENSPCOG00000024872.1.
DR   GeneTree; ENSGT00940000159439; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR   GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IEA:Ensembl.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:Ensembl.
DR   CDD; cd01369; KISc_KHC_KIF5; 1.
DR   Gene3D; 6.10.250.1590; -; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF56; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 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:UP000233160}.
FT   DOMAIN          9..328
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          909..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          333..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          415..540
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          592..893
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        970..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86..93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1024 AA;  116434 MW;  DAC753D1F29AB5A9 CRC64;
     MAETNNECSI KVLCRFRPLN QAEILRGDKF IPIFQGDDSV VIGGKPYVFD RVFPPNTTQE
     QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIARDIFNHI
     YSMDENLEFH IKVTGMEAQV LLTLHSLDLV TKTNLSVHED KNRVPFVKGC TERFVSSPEE
     ILDVIDEGKS NRHVAVTNMN EHSSRSHSIF LINIKQENME TEQKLSGKLY LVDLAGSEKV
     SKTGAEGAVL DEAKNINKSL SALGNVISAL AEGTKSYVPY RDSKMTRILQ DSLGGNCRTT
     MFICCSPSSY NDAETKSTLM FGQRAKTIKN TASVNLELTA EQWKKKYEKE KEKTKAQKET
     IAKLEAELSR WRNGENVPET ERLAGEDAGL GAELCEETPV NDNSSIVVRI APEERQKYEE
     EIRRLYKQLD DKDDEINQQS QLIEKLKQQM LDQEELLVST RGDNEKVQRE LSHLQSENDA
     AKDEVKEVLQ ALEELAVNYD QKSQEVEEKS QQNQLLVDEL SQKVATMLSL ESELQRLQEV
     SGHQRKRIAE VLNGLMKDLS EFSVIVGNGE IKLPVEISGA IEEEFTVARL YISKIKSEVK
     SVVKRCRQLE NLQVECHRKM EVTGRELSSC QLLISQHEAK IRSLTEYMQS VELKKRHLEE
     SYDSLSDELA KLQAQETVHE VALKDKEPDT QDADEVKKAL ELQMENHREA HHRQLARLRD
     EINEKQKTID ELKDLNQKLQ LELEKLQADY EKLKNEEHEK STKLQELTFL YERHEQSKQD
     LKGLEETVAR ELQTLHNLRK LFVQDVTTRV KKSAEMEPED SGGIHSQKQK ISFLENNLEQ
     LTKVHKQLVR DNADLRCELP KLEKRLRATA ERVKALEGAL KEDKRRYQQE EAVRYKSSVP
     RCQLHDLRGH AKPVRPGHYP ASSPTNPYGT RSPECISYTN SLFQNYQNLY LQPTPSSTSD
     MYFSNSCTSS GATSSGGPLA SYQKANMDNG NATDINDNRS DLPCGYEAED QAKLFPLHQE
     TAAS
//