ID   KIF5C_HUMAN             Reviewed;         957 AA.
AC   O60282; O95079; Q2YDC5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Kinesin heavy chain isoform 5C;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P56536};
DE   AltName: Full=Kinesin heavy chain neuron-specific 2;
DE   AltName: Full=Kinesin-1 {ECO:0000250|UniProtKB:P56536};
GN   Name=KIF5C; Synonyms=KIAA0531, NKHC2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 355-585 (ISOFORMS 1/2).
RX   PubMed=9361024; DOI=10.1093/hmg/6.13.2205;
RA   Engelender S., Sharp A.H., Colomer V., Tokito M.K., Lanahan A., Worley P.,
RA   Holzbaur E.L.F., Ross C.A.;
RT   "Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued
RT   subunit of dynactin.";
RL   Hum. Mol. Genet. 6:2205-2212(1997).
RN   [5]
RP   INTERACTION WITH TRAK1.
RX   PubMed=15644324; DOI=10.1074/jbc.m409095200;
RA   Brickley K., Smith M.J., Beck M., Stephenson F.A.;
RT   "GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain
RT   proteins: association in vivo and in vitro with kinesin.";
RL   J. Biol. Chem. 280:14723-14732(2005).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, VARIANT CDCBM2 LYS-237, AND
RP   CHARACTERIZATION OF VARIANT CDCBM2 LYS-237.
RX   PubMed=24812067; DOI=10.1136/jmedgenet-2013-102182;
RA   Willemsen M.H., Ba W., Wissink-Lindhout W.M., de Brouwer A.P., Haas S.A.,
RA   Bienek M., Hu H., Vissers L.E., van Bokhoven H., Kalscheuer V.,
RA   Nadif Kasri N., Kleefstra T.;
RT   "Involvement of the kinesin family members KIF4A and KIF5C in intellectual
RT   disability and synaptic function.";
RL   J. Med. Genet. 51:487-494(2014).
RN   [8]
RP   VARIANT CDCBM2 LYS-237.
RX   PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA   de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA   Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA   del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA   Veltman J.A., Vissers L.E.;
RT   "Diagnostic exome sequencing in persons with severe intellectual
RT   disability.";
RL   N. Engl. J. Med. 367:1921-1929(2012).
RN   [9]
RP   VARIANT CDCBM2 VAL-237, AND CHARACTERIZATION OF VARIANT CDCBM2 VAL-237.
RX   PubMed=23603762; DOI=10.1038/ng.2613;
RA   Poirier K., Lebrun N., Broix L., Tian G., Saillour Y., Boscheron C.,
RA   Parrini E., Valence S., Pierre B.S., Oger M., Lacombe D., Genevieve D.,
RA   Fontana E., Darra F., Cances C., Barth M., Bonneau D., Bernadina B.D.,
RA   N'guyen S., Gitiaux C., Parent P., des Portes V., Pedespan J.M., Legrez V.,
RA   Castelnau-Ptakine L., Nitschke P., Hieu T., Masson C., Zelenika D.,
RA   Andrieux A., Francis F., Guerrini R., Cowan N.J., Bahi-Buisson N.,
RA   Chelly J.;
RT   "Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of
RT   cortical development and microcephaly.";
RL   Nat. Genet. 45:639-647(2013).
RN   [10]
RP   VARIANT CDCBM2 LYS-237.
RX   PubMed=29048727; DOI=10.1002/ajmg.a.38496;
RA   Michels S., Foss K., Park K., Golden-Grant K., Saneto R., Lopez J.,
RA   Mirzaa G.M.;
RT   "Mutations of KIF5C cause a neurodevelopmental disorder of infantile-onset
RT   epilepsy, absent language, and distinctive malformations of cortical
RT   development.";
RL   Am. J. Med. Genet. A 173:3127-3131(2017).
CC   -!- FUNCTION: Microtubule-associated force-producing protein that may play
CC       a role in organelle transport. Has ATPase activity (By similarity).
CC       Involved in synaptic transmission (PubMed:24812067). Mediates dendritic
CC       trafficking of mRNAs (By similarity). Required for anterograde axonal
CC       transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3
CC       function in axon elongation (By similarity).
CC       {ECO:0000250|UniProtKB:P28738, ECO:0000250|UniProtKB:P56536,
CC       ECO:0000269|PubMed:24812067}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P56536};
CC   -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC       Interacts with GRIP1 and KLC3 (By similarity). Interacts with TRAK1
CC       (PubMed:15644324). Interacts with ZFYVE27 (By similarity).
CC       {ECO:0000250|UniProtKB:P28738, ECO:0000250|UniProtKB:P56536,
CC       ECO:0000269|PubMed:15644324}.
CC   -!- INTERACTION:
CC       O60282; P68400: CSNK2A1; NbExp=4; IntAct=EBI-717170, EBI-347804;
CC       O60282; P19784: CSNK2A2; NbExp=4; IntAct=EBI-717170, EBI-347451;
CC       O60282; Q8IXI2: RHOT1; NbExp=2; IntAct=EBI-717170, EBI-1396430;
CC       O60282-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12334027, EBI-16439278;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC       projection, dendrite {ECO:0000269|PubMed:24812067}. Note=Abundant in
CC       distal regions of dendrites. {ECO:0000269|PubMed:24812067}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O60282-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60282-2; Sequence=VSP_035715, VSP_035716;
CC   -!- TISSUE SPECIFICITY: Highest expression in brain, prostate and testis,
CC       and moderate expression in kidney, small intestine and ovary.
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   -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 2
CC       (CDCBM2) [MIM:615282]: A disorder of aberrant neuronal migration and
CC       disturbed axonal guidance. Clinical features include intrauterine
CC       growth retardation, fetal akinesia, seizures, microcephaly, lack of
CC       psychomotor development, and arthrogryposis. Brain imaging shows
CC       malformations of cortical development, including polymicrogyria, gyral
CC       simplification, and thin corpus callosum. {ECO:0000269|PubMed:23033978,
CC       ECO:0000269|PubMed:23603762, ECO:0000269|PubMed:24812067,
CC       ECO:0000269|PubMed:29048727}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25457.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB011103; BAA25457.2; ALT_INIT; mRNA.
DR   EMBL; AC105402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC144443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC144611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC110287; AAI10288.1; -; mRNA.
DR   EMBL; AF010146; AAD01436.1; -; mRNA.
DR   CCDS; CCDS74586.1; -. [O60282-1]
DR   RefSeq; NP_004513.1; NM_004522.2. [O60282-1]
DR   RefSeq; XP_011509459.1; XM_011511157.2. [O60282-2]
DR   RefSeq; XP_016859551.1; XM_017004062.1. [O60282-1]
DR   AlphaFoldDB; O60282; -.
DR   SMR; O60282; -.
DR   BioGRID; 110001; 67.
DR   CORUM; O60282; -.
DR   IntAct; O60282; 50.
DR   MINT; O60282; -.
DR   STRING; 9606.ENSP00000393379; -.
DR   BindingDB; O60282; -.
DR   ChEMBL; CHEMBL2029194; -.
DR   iPTMnet; O60282; -.
DR   PhosphoSitePlus; O60282; -.
DR   SwissPalm; O60282; -.
DR   BioMuta; KIF5C; -.
DR   EPD; O60282; -.
DR   jPOST; O60282; -.
DR   MassIVE; O60282; -.
DR   MaxQB; O60282; -.
DR   PaxDb; 9606-ENSP00000393379; -.
DR   PeptideAtlas; O60282; -.
DR   ProteomicsDB; 49311; -. [O60282-1]
DR   ProteomicsDB; 49312; -. [O60282-2]
DR   Pumba; O60282; -.
DR   Antibodypedia; 33631; 176 antibodies from 22 providers.
DR   DNASU; 3800; -.
DR   Ensembl; ENST00000435030.6; ENSP00000393379.1; ENSG00000168280.18. [O60282-1]
DR   Ensembl; ENST00000676677.1; ENSP00000503401.1; ENSG00000168280.18. [O60282-2]
DR   Ensembl; ENST00000677891.1; ENSP00000503013.1; ENSG00000168280.18. [O60282-1]
DR   Ensembl; ENST00000679129.1; ENSP00000504291.1; ENSG00000168280.18. [O60282-2]
DR   GeneID; 3800; -.
DR   KEGG; hsa:3800; -.
DR   MANE-Select; ENST00000435030.6; ENSP00000393379.1; NM_004522.3; NP_004513.1.
DR   UCSC; uc010zbu.3; human. [O60282-1]
DR   AGR; HGNC:6325; -.
DR   CTD; 3800; -.
DR   DisGeNET; 3800; -.
DR   GeneCards; KIF5C; -.
DR   HGNC; HGNC:6325; KIF5C.
DR   HPA; ENSG00000168280; Tissue enriched (brain).
DR   MalaCards; KIF5C; -.
DR   MIM; 604593; gene.
DR   MIM; 615282; phenotype.
DR   neXtProt; NX_O60282; -.
DR   OpenTargets; ENSG00000168280; -.
DR   PharmGKB; PA30109; -.
DR   VEuPathDB; HostDB:ENSG00000168280; -.
DR   eggNOG; KOG0240; Eukaryota.
DR   GeneTree; ENSGT00940000158539; -.
DR   HOGENOM; CLU_001485_11_1_1; -.
DR   InParanoid; O60282; -.
DR   OMA; QKSAEPY; -.
DR   OrthoDB; 5476186at2759; -.
DR   PhylomeDB; O60282; -.
DR   TreeFam; TF105225; -.
DR   PathwayCommons; O60282; -.
DR   Reactome; R-HSA-264876; Insulin processing.
DR   SignaLink; O60282; -.
DR   SIGNOR; O60282; -.
DR   BioGRID-ORCS; 3800; 7 hits in 389 CRISPR screens.
DR   ChiTaRS; KIF5C; human.
DR   GeneWiki; KIF5C; -.
DR   GenomeRNAi; 3800; -.
DR   Pharos; O60282; Tbio.
DR   PRO; PR:O60282; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; O60282; Protein.
DR   Bgee; ENSG00000168280; Expressed in Brodmann (1909) area 10 and 162 other cell types or tissues.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0044295; C:axonal growth cone; ISS:ARUK-UCL.
DR   GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR   GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR   GO; GO:0150034; C:distal axon; ISS:ARUK-UCL.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR   GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR   GO; GO:0034190; F:apolipoprotein receptor binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; TAS:ProtInc.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR   GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; IEA:Ensembl.
DR   GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0008298; P:intracellular mRNA localization; IEA:Ensembl.
DR   GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR   GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
DR   GO; GO:0006996; P:organelle organization; TAS:ProtInc.
DR   GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
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:SF57; KINESIN FAMILY MEMBER 5C; 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.
DR   Genevisible; O60282; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Disease variant; Hydrolase; Microtubule; Motor protein;
KW   Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..957
FT                   /note="Kinesin heavy chain isoform 5C"
FT                   /id="PRO_0000125355"
FT   DOMAIN          8..327
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          174..315
FT                   /note="Microtubule-binding"
FT   REGION          859..956
FT                   /note="Globular"
FT   REGION          911..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          406..923
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P56536"
FT   VAR_SEQ         1..232
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035715"
FT   VAR_SEQ         233..238
FT                   /note="LAGSEK -> MATYIH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035716"
FT   VARIANT         237
FT                   /note="E -> K (in CDCBM2; the mutation results in a
FT                   significant decrease of excitatory post-synaptic currents
FT                   when expressed in cultured primary hippocampal neurons;
FT                   decreased localization to distal regions of dendrites;
FT                   accumulates in dendrite cell body; dbSNP:rs587777570)"
FT                   /evidence="ECO:0000269|PubMed:23033978,
FT                   ECO:0000269|PubMed:24812067, ECO:0000269|PubMed:29048727"
FT                   /id="VAR_069389"
FT   VARIANT         237
FT                   /note="E -> V (in CDCBM2; the mutant protein has a complete
FT                   loss of ATP hydrolysis activity; colocalizes with
FT                   microtubules throughout the cell but does not appear as
FT                   puncta or accumulates in cortical clusters as does the
FT                   wild-type protein; dbSNP:rs587777035)"
FT                   /evidence="ECO:0000269|PubMed:23603762"
FT                   /id="VAR_070574"
FT   CONFLICT        355..360
FT                   /note="TLKNVI -> STHASV (in Ref. 4; AAD01436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        583..585
FT                   /note="EFT -> DRV (in Ref. 4; AAD01436)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   957 AA;  109495 MW;  A9F25BB1C994322A CRC64;
     MADPAECSIK VMCRFRPLNE AEILRGDKFI PKFKGDETVV IGQGKPYVFD RVLPPNTTQE
     QVYNACAKQI VKDVLEGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIAHDIFDHI
     YSMDENLEFH IKVSYFEIYL DKIRDLLDVS KTNLAVHEDK NRVPYVKGCT ERFVSSPEEV
     MDVIDEGKAN RHVAVTNMNE HSSRSHSIFL INIKQENVET EKKLSGKLYL VDLAGSEKVS
     KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKTHVPYR DSKMTRILQD SLGGNCRTTI
     VICCSPSVFN EAETKSTLMF GQRAKTIKNT VSVNLELTAE EWKKKYEKEK EKNKTLKNVI
     QHLEMELNRW RNGEAVPEDE QISAKDQKNL EPCDNTPIID NIAPVVAGIS TEEKEKYDEE
     ISSLYRQLDD KDDEINQQSQ LAEKLKQQML DQDELLASTR RDYEKIQEEL TRLQIENEAA
     KDEVKEVLQA LEELAVNYDQ KSQEVEDKTR ANEQLTDELA QKTTTLTTTQ RELSQLQELS
     NHQKKRATEI LNLLLKDLGE IGGIIGTNDV KTLADVNGVI EEEFTMARLY ISKMKSEVKS
     LVNRSKQLES AQMDSNRKMN ASERELAACQ LLISQHEAKI KSLTDYMQNM EQKRRQLEES
     QDSLSEELAK LRAQEKMHEV SFQDKEKEHL TRLQDAEEMK KALEQQMESH REAHQKQLSR
     LRDEIEEKQK IIDEIRDLNQ KLQLEQEKLS SDYNKLKIED QEREMKLEKL LLLNDKREQA
     REDLKGLEET VSRELQTLHN LRKLFVQDLT TRVKKSVELD NDDGGGSAAQ KQKISFLENN
     LEQLTKVHKQ LVRDNADLRC ELPKLEKRLR ATAERVKALE SALKEAKENA MRDRKRYQQE
     VDRIKEAVRA KNMARRAHSA QIAKPIRPGH YPASSPTAVH AIRGGGGSSS NSTHYQK
//