ID   KIF5A_PONAB             Reviewed;        1032 AA.
AC   Q5R9K7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Kinesin heavy chain isoform 5A;
GN   Name=KIF5A;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Microtubule-dependent motor required for slow axonal
CC       transport of neurofilament proteins (NFH, NFM and NFL). Can induce
CC       formation of neurite-like membrane protrusions in non-neuronal cells in
CC       a ZFYVE27-dependent manner. The ZFYVE27-KIF5A complex contributes to
CC       the vesicular transport of VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3
CC       proteins in neurons. Required for anterograde axonal transportation of
CC       MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon
CC       elongation. {ECO:0000250|UniProtKB:P33175,
CC       ECO:0000250|UniProtKB:Q6QLM7}.
CC   -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC       Interacts with GRIP1. Interacts with FMR1 (via C-terminus); this
CC       interaction is increased in a mGluR-dependent manner. Interacts with
CC       BORCS5. Interacts with ZFYVE27. Interacts with VAPA, VAPB, SURF4,
CC       RAB11A (GDP-bound form), RAB11B (GDP-bound form) and RTN3 in a ZFYVE27-
CC       dependent manner. Interacts with BICD2. Interacts with DTNB (By
CC       similarity). {ECO:0000250|UniProtKB:P33175,
CC       ECO:0000250|UniProtKB:Q12840}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q6QLM7}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q6QLM7}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q6QLM7}. Note=Concentrated in the cell body of
CC       the neurons, particularly in the perinuclear region.
CC       {ECO:0000250|UniProtKB:Q6QLM7}.
CC   -!- DOMAIN: Composed of three structural domains: a large globular N-
CC       terminal domain which is responsible for the motor activity of kinesin
CC       (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC       coiled coil domain that mediates the heavy chain dimerization; and a
CC       small globular C-terminal domain which interacts with other proteins
CC       (such as the kinesin light chains), vesicles and membranous organelles.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; CR859380; CAH91553.1; -; mRNA.
DR   RefSeq; NP_001125912.1; NM_001132440.1.
DR   AlphaFoldDB; Q5R9K7; -.
DR   SMR; Q5R9K7; -.
DR   STRING; 9601.ENSPPYP00000005348; -.
DR   GeneID; 100172845; -.
DR   KEGG; pon:100172845; -.
DR   CTD; 3798; -.
DR   eggNOG; KOG0240; Eukaryota.
DR   InParanoid; Q5R9K7; -.
DR   OrthoDB; 1334528at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR   Gene3D; 3.40.850.10; -; 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; PTHR24115; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q12840"
FT   CHAIN           2..1032
FT                   /note="Kinesin heavy chain isoform 5A"
FT                   /id="PRO_0000230789"
FT   DOMAIN          9..327
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          174..315
FT                   /note="Microtubule-binding"
FT   REGION          271..361
FT                   /note="Necessary for interaction with ZFYVE27"
FT                   /evidence="ECO:0000250|UniProtKB:P33175"
FT   REGION          353..1032
FT                   /note="Interaction with BICD2"
FT                   /evidence="ECO:0000250|UniProtKB:Q12840"
FT   REGION          904..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..1032
FT                   /note="Globular"
FT   COILED          331..906
FT   BINDING         86..93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12840"
FT   MOD_RES         397
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P33175"
SQ   SEQUENCE   1032 AA;  117357 MW;  9EE8852A415CF458 CRC64;
     MAETNNECSI KVLCRFRPLN QAEILRGDKF IPIFQGDDSV VIGGKPYVFD RVFPPNTTQE
     QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIARDIFNHI
     YSMDENLEFH IKVSYFEIYL DKIRDLLDVT KTNLSVHEDK NRVPFVKGCT ERFVSGPEEI
     LDVIDEGKSN RHVAVTNMNE HSSRSHSIFL INIKQENMET EQKLSGKLYL VDLAGSEKVS
     KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKSYVPYR DSKMTRILQD SLGGNCRTTM
     FICCSPSSYN DAETKSTLMF GQRAKTIKNT ASVNLELTAE QWKKKYEKEK EKTKAQKETI
     AKLEAELSRW RNGENVPETE RLAGEEAALG AELCEETPVN DNSSIVVRIA PEERQKYEEE
     IRRLYKQLDD KDDEINQQSQ LIEKLKQQML DQEELLVSTR GDNEKVQQEL SHLQSENDAA
     KDEVKEVLQA LEELAVNYDQ KSQEVEEKSQ QNQLLVDELS QKVATMLSLE SELQRLQEVS
     GHQRKRIAEV LNGLMKDLSE FSVIVGNGEI KLPVEISGAI EEEFTVARLY ISKIKSEVKS
     VVKRCRQLEN LQVERHRKME VTGRELSSCQ LLISQHEAKI RSLTEYMQSV ELKKRHLEES
     YDSLSDELAK LQAQETVHEV ALKDKEPDTQ DADEVKKALE LQMESHREAH HRQLARLRDE
     INEKQKTIDE LKDLNQKLQL ELEKLQADYE KLKSEEHEKS TKLQELTFLY ERHEQSKQDL
     KGLEETVARE LQTLHNLRKL FVQDVTTRVK KSAEMEPEDS GGIHSQKQKI SFLENNLEQL
     TKVHKQLVRD NADLRCELPK LEKRLRATAE RVKALEGALK EAKEGAMKDK RRYQQEVDRI
     KEAVRYKSSG KRGHSAQIAK PVRPGHYPAS SPTNPYGTRS PECISYTNSL FQNYQNLYLQ
     ATPSSTSDMY FANSCTGSGA TSSGGPLASY QKANMDNGNA TDIKDNRSDL PCGYEAEDQA
     KLFPLHQETA AS