KIF1A_HUMAN
ID KIF1A_HUMAN Reviewed; 1690 AA.
AC Q12756; B0I1S5; F5H045; O95068; Q13355; Q14752; Q2NKJ6; Q4LE42; Q53T78;
AC Q59GH1; Q63Z40; Q6P1R9; Q7KZ57;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Kinesin-like protein KIF1A;
DE AltName: Full=Axonal transporter of synaptic vesicles;
DE AltName: Full=Microtubule-based motor KIF1A;
DE AltName: Full=Unc-104- and KIF1A-related protein;
DE Short=hUnc-104;
GN Name=KIF1A; Synonyms=ATSV, C2orf20;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8661001; DOI=10.1006/geno.1996.0217;
RA Furlong R.A., Zhou C.Y., Ferguson-Smith M.A., Affara N.A.;
RT "Characterization of a kinesin-related gene ATSV, within the tuberous
RT sclerosis locus (TSC1) candidate region on chromosome 9q34.";
RL Genomics 33:421-429(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
RT "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
RT recombination: preparation of full-length cDNA clones encoding motor
RT proteins.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1362 (ISOFORM 2).
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 102-251.
RC TISSUE=Retina;
RA Bost-Usinger L., Hoang E.H.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 882-1690 (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1030-1690 (ISOFORM 1).
RC TISSUE=Brain;
RA Campagna S.E., Otsuka A.J.;
RT "A putative human kinesin family member with sequence similarity to unc-104
RT and KIF1A.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1275-1690 (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1318-1690 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP INVOLVEMENT IN HSN2C.
RX PubMed=21820098; DOI=10.1016/j.ajhg.2011.06.013;
RA Riviere J.B., Ramalingam S., Lavastre V., Shekarabi M., Holbert S.,
RA Lafontaine J., Srour M., Merner N., Rochefort D., Hince P., Gaudet R.,
RA Mes-Masson A.M., Baets J., Houlden H., Brais B., Nicholson G.A.,
RA Van Esch H., Nafissi S., De Jonghe P., Reilly M.M., Timmerman V.,
RA Dion P.A., Rouleau G.A.;
RT "KIF1A, an axonal transporter of synaptic vesicles, is mutated in
RT hereditary sensory and autonomic neuropathy type 2.";
RL Am. J. Hum. Genet. 89:219-230(2011).
RN [12]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT NESCAVS MET-99, AND
RP CHARACTERIZATION OF VARIANT NESCAVS MET-99.
RX PubMed=21376300; DOI=10.1016/j.ajhg.2011.02.001;
RA Hamdan F.F., Gauthier J., Araki Y., Lin D.T., Yoshizawa Y., Higashi K.,
RA Park A.R., Spiegelman D., Dobrzeniecka S., Piton A., Tomitori H., Daoud H.,
RA Massicotte C., Henrion E., Diallo O., Shekarabi M., Marineau C.,
RA Shevell M., Maranda B., Mitchell G., Nadeau A., D'Anjou G., Vanasse M.,
RA Srour M., Lafreniere R.G., Drapeau P., Lacaille J.C., Kim E., Lee J.R.,
RA Igarashi K., Huganir R.L., Rouleau G.A., Michaud J.L.;
RT "Excess of de novo deleterious mutations in genes associated with
RT glutamatergic systems in nonsyndromic intellectual disability.";
RL Am. J. Hum. Genet. 88:306-316(2011).
RN [13]
RP ERRATUM OF PUBMED:21376300.
RA Hamdan F.F., Gauthier J., Araki Y., Lin D.T., Yoshizawa Y., Higashi K.,
RA Park A.R., Spiegelman D., Dobrzeniecka S., Piton A., Tomitori H., Daoud H.,
RA Massicotte C., Henrion E., Diallo O., Shekarabi M., Marineau C.,
RA Shevell M., Maranda B., Mitchell G., Nadeau A., D'Anjou G., Vanasse M.,
RA Srour M., Lafreniere R.G., Drapeau P., Lacaille J.C., Kim E., Lee J.R.,
RA Igarashi K., Huganir R.L., Rouleau G.A., Michaud J.L.;
RL Am. J. Hum. Genet. 88:516-516(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-418; SER-419;
RP SER-937; SER-1310 AND SER-1548, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP INTERACTION WITH CALM1; PPFIA2 AND TANC2.
RX PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071;
RA Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I.,
RA Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.;
RT "Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls
RT DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.";
RL Cell Rep. 24:685-700(2018).
RN [16]
RP INVOLVEMENT IN SPG30, AND VARIANT SPG30 LEU-69.
RX PubMed=25585697; DOI=10.1038/ejhg.2014.297;
RA Ylikallio E., Kim D., Isohanni P., Auranen M., Kim E., Loennqvist T.,
RA Tyynismaa H.;
RT "Dominant transmission of de novo KIF1A motor domain variant underlying
RT pure spastic paraplegia.";
RL Eur. J. Hum. Genet. 23:1427-1430(2015).
RN [17]
RP INVOLVEMENT IN SPG30, AND VARIANTS SPG30 LEU-69; SER-102; CYS-167 AND
RP THR-1026.
RX PubMed=26410750; DOI=10.1007/s00415-015-7899-9;
RA Citterio A., Arnoldi A., Panzeri E., Merlini L., D'Angelo M.G.,
RA Musumeci O., Toscano A., Bondi A., Martinuzzi A., Bresolin N., Bassi M.T.;
RT "Variants in KIF1A gene in dominant and sporadic forms of hereditary
RT spastic paraparesis.";
RL J. Neurol. 262:2684-2690(2015).
RN [18]
RP VARIANT SPG30 VAL-255.
RX PubMed=21487076; DOI=10.1101/gr.117143.110;
RA Erlich Y., Edvardson S., Hodges E., Zenvirt S., Thekkat P., Shaag A.,
RA Dor T., Hannon G.J., Elpeleg O.;
RT "Exome sequencing and disease-network analysis of a single family implicate
RT a mutation in KIF1A in hereditary spastic paraparesis.";
RL Genome Res. 21:658-664(2011).
RN [19]
RP VARIANTS SPG30 VAL-255 AND GLY-350.
RX PubMed=22258533; DOI=10.1038/ejhg.2011.261;
RA Klebe S., Lossos A., Azzedine H., Mundwiller E., Sheffer R., Gaussen M.,
RA Marelli C., Nawara M., Carpentier W., Meyer V., Rastetter A., Martin E.,
RA Bouteiller D., Orlando L., Gyapay G., El-Hachimi K.H., Zimmerman B.,
RA Gamliel M., Misk A., Lerer I., Brice A., Durr A., Stevanin G.;
RT "KIF1A missense mutations in SPG30, an autosomal recessive spastic
RT paraplegia: distinct phenotypes according to the nature of the mutations.";
RL Eur. J. Hum. Genet. 20:645-649(2012).
RN [20]
RP VARIANTS MET-46; ASN-136; ILE-187; MET-205; ILE-220; ASP-233; VAL-336 AND
RP HIS-355, VARIANTS NESCAVS MET-99; CYS-216; HIS-216; LYS-253 AND TRP-316,
RP CHARACTERIZATION OF VARIANTS NESCAVS MET-99; CYS-216 AND LYS-253,
RP CHARACTERIZATION OF VARIANT SPG30 VAL-255, AND CHARACTERIZATION OF VARIANT
RP ILE-220.
RX PubMed=26125038; DOI=10.1002/acn3.198;
RA Esmaeeli Nieh S., Madou M.R., Sirajuddin M., Fregeau B., McKnight D.,
RA Lexa K., Strober J., Spaeth C., Hallinan B.E., Smaoui N., Pappas J.G.,
RA Burrow T.A., McDonald M.T., Latibashvili M., Leshinsky-Silver E., Lev D.,
RA Blumkin L., Vale R.D., Barkovich A.J., Sherr E.H.;
RT "De novo mutations in KIF1A cause progressive encephalopathy and brain
RT atrophy.";
RL Ann. Clin. Transl. Neurol. 2:623-635(2015).
RN [21]
RP VARIANTS NESCAVS ASP-148; GLN-254; TRP-254; GLN-307 AND TRP-316.
RX PubMed=26354034; DOI=10.1038/jhg.2015.108;
RA Ohba C., Haginoya K., Osaka H., Kubota K., Ishiyama A., Hiraide T.,
RA Komaki H., Sasaki M., Miyatake S., Nakashima M., Tsurusaki Y., Miyake N.,
RA Tanaka F., Saitsu H., Matsumoto N.;
RT "De novo KIF1A mutations cause intellectual deficit, cerebellar atrophy,
RT lower limb spasticity and visual disturbance.";
RL J. Hum. Genet. 60:739-742(2015).
RN [22]
RP VARIANTS NESCAVS LEU-58; MET-99; ASP-102; PHE-144; CYS-167; PRO-202;
RP ARG-215; PRO-216; GLN-249; LYS-253 AND TRP-316, CHARACTERIZATION OF
RP VARIANTS NESCAVS MET-99; PRO-202; ARG-215; PRO-216 AND LYS-253,
RP CHARACTERIZATION OF VARIANTS SPG30 VAL-255 AND GLY-350, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25265257; DOI=10.1002/humu.22709;
RA Lee J.R., Srour M., Kim D., Hamdan F.F., Lim S.H., Brunel-Guitton C.,
RA Decarie J.C., Rossignol E., Mitchell G.A., Schreiber A., Moran R.,
RA Van Haren K., Richardson R., Nicolai J., Oberndorff K.M., Wagner J.D.,
RA Boycott K.M., Rahikkala E., Junna N., Tyynismaa H., Cuppen I.,
RA Verbeek N.E., Stumpel C.T., Willemsen M.A., de Munnik S.A., Rouleau G.A.,
RA Kim E., Kamsteeg E.J., Kleefstra T., Michaud J.L.;
RT "De novo mutations in the motor domain of KIF1A cause cognitive impairment,
RT spastic paraparesis, axonal neuropathy, and cerebellar atrophy.";
RL Hum. Mutat. 36:69-78(2015).
RN [23]
RP VARIANTS NESCAVS ARG-199 AND GLN-307.
RX PubMed=27034427; DOI=10.1177/0883073816639718;
RA Hotchkiss L., Donkervoort S., Leach M.E., Mohassel P.,
RA Bharucha-Goebel D.X., Bradley N., Nguyen D., Hu Y., Gurgel-Giannetti J.,
RA Boennemann C.G.;
RT "Novel De Novo Mutations in KIF1A as a Cause of Hereditary Spastic
RT Paraplegia With Progressive Central Nervous System Involvement.";
RL J. Child Neurol. 31:1114-1119(2016).
RN [24]
RP VARIANT SPG30 LEU-69.
RX PubMed=29159194; DOI=10.1002/acn3.452;
RA Roda R.H., Schindler A.B., Blackstone C.;
RT "Multigeneration family with dominant SPG30 hereditary spastic
RT paraplegia.";
RL Ann. Clin. Transl. Neurol. 4:821-824(2017).
RN [25]
RP VARIANT SPG30 TRP-11.
RX PubMed=28832565; DOI=10.1038/ejhg.2017.124;
RA Morais S., Raymond L., Mairey M., Coutinho P., Brandao E., Ribeiro P.,
RA Loureiro J.L., Sequeiros J., Brice A., Alonso I., Stevanin G.;
RT "Massive sequencing of 70 genes reveals a myriad of missing genes or
RT mechanisms to be uncovered in hereditary spastic paraplegias.";
RL Eur. J. Hum. Genet. 25:1217-1228(2017).
RN [26]
RP VARIANTS SPG30 THR-30; CYS-56; LEU-69; CYS-74; SER-78; ASN-106; HIS-167;
RP PRO-173; ARG-252; MET-258; TRP-350; GLY-460; 623-GLN--VAL-1690 DEL;
RP CYS-843; LYS-859 AND 1325-TYR--VAL-1690 DEL.
RX PubMed=31488895; DOI=10.1038/s41431-019-0497-z;
RA Pennings M., Schouten M.I., van Gaalen J., Meijer R.P.P., de Bot S.T.,
RA Kriek M., Saris C.G.J., van den Berg L.H., van Es M.A., Zuidgeest D.M.H.,
RA Elting M.W., van de Kamp J.M., van Spaendonck-Zwarts K.Y., Die-Smulders C.,
RA Brilstra E.H., Verschuuren C.C., de Vries B.B.A., Bruijn J., Sofou K.,
RA Duijkers F.A., Jaeger B., Schieving J.H., van de Warrenburg B.P.,
RA Kamsteeg E.J.;
RT "KIF1A variants are a frequent cause of autosomal dominant hereditary
RT spastic paraplegia.";
RL Eur. J. Hum. Genet. 28:40-49(2020).
RN [27]
RP VARIANTS SPG30 GLN-11 AND LEU-69, AND VARIANTS NESCAVS PHE-186; LYS-253;
RP TRP-254; PRO-307 AND PRO-323.
RX PubMed=32096284; DOI=10.1111/jns.12368;
RG Genomics England Research Consortium;
RA Nemani T., Steel D., Kaliakatsos M., DeVile C., Ververi A., Scott R.,
RA Getov S., Sudhakar S., Male A., Mankad K., Muntoni F., Reilly M.M.,
RA Kurian M.A., Carr L., Munot P.;
RT "KIF1A-related disorders in children: A wide spectrum of central and
RT peripheral nervous system involvement.";
RL J. Peripher. Nerv. Syst. 25:117-124(2020).
RN [28]
RP VARIANTS NESCAVS CYS-216 AND TRP-380.
RX PubMed=31805580; DOI=10.1055/s-0039-3400988;
RA Van Beusichem A.E., Nicolai J., Verhoeven J., Speth L., Coenen M.,
RA Willemsen M.A., Kamsteeg E.J., Stumpel C., Vermeulen R.J.;
RT "Mobility characteristics of children with spastic paraplegia due to a
RT mutation in the KIF1A gene.";
RL Neuropediatrics 51:146-153(2020).
CC -!- FUNCTION: Motor for anterograde axonal transport of synaptic vesicle
CC precursors. Also required for neuronal dense core vesicles (DCVs)
CC transport to the dendritic spines and axons. The interaction calcium-
CC dependent with CALM1 increases vesicle motility and interaction with
CC the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic
CC sites. {ECO:0000250|UniProtKB:F1M4A4}.
CC -!- SUBUNIT: Monomer. Interacts with PPFIA1 and PPFIA4 (By similarity).
CC Interacts with CALM1; the interaction is increased in presence of
CC calcium and increases neuronal dense core vesicles motility
CC (PubMed:30021165). Interacts with PPFIA2 and TANC2; both interactions
CC allow the recruitment of neuronal dense core vesicles to dendritic
CC spines and decrease in presence of calcium (PubMed:30021165). Interacts
CC with SYT4 (unphosphorylated) and SYT11; both interactions increase in
CC presence of calcium (By similarity). Interacts with MADD (By
CC similarity). {ECO:0000250|UniProtKB:F1M4A4,
CC ECO:0000250|UniProtKB:P33173, ECO:0000269|PubMed:30021165}.
CC -!- INTERACTION:
CC Q12756; P07339: CTSD; NbExp=3; IntAct=EBI-2679809, EBI-2115097;
CC Q12756; P28799: GRN; NbExp=3; IntAct=EBI-2679809, EBI-747754;
CC Q12756; Q12756: KIF1A; NbExp=4; IntAct=EBI-2679809, EBI-2679809;
CC Q12756; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2679809, EBI-10975473;
CC Q12756; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2679809, EBI-5235340;
CC Q12756; P02766: TTR; NbExp=3; IntAct=EBI-2679809, EBI-711909;
CC Q12756; O76024: WFS1; NbExp=3; IntAct=EBI-2679809, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21376300}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:25265257}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P33173}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P33173}. Synapse {ECO:0000250|UniProtKB:P33173}.
CC Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle
CC membrane {ECO:0000250|UniProtKB:F1M4A4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:F1M4A4}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:F1M4A4}. Note=Within neuronal cells concentrated
CC in the axon, with smaller amounts in the perinuclear and synaptic
CC regions (By similarity). Expressed in distal regions of neurites.
CC {ECO:0000250|UniProtKB:P33173, ECO:0000269|PubMed:25265257}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q12756-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12756-2; Sequence=VSP_021853, VSP_021854, VSP_021855;
CC Name=3;
CC IsoId=Q12756-3; Sequence=VSP_021853, VSP_021854;
CC -!- TISSUE SPECIFICITY: Expressed in neurons.
CC {ECO:0000269|PubMed:21376300}.
CC -!- DISEASE: Spastic paraplegia 30 (SPG30) [MIM:610357]: A form of spastic
CC paraplegia, a neurodegenerative disorder characterized by a slow,
CC gradual, progressive weakness and spasticity of the lower limbs. Rate
CC of progression and the severity of symptoms are quite variable. Initial
CC symptoms may include difficulty with balance, weakness and stiffness in
CC the legs, muscle spasms, and dragging the toes when walking. In some
CC forms of the disorder, bladder symptoms (such as incontinence) may
CC appear, or the weakness and stiffness may spread to other parts of the
CC body. Some SPG30 patients have a pure form of the disorder, limited to
CC spastic paraplegia, whereas others may have a complicated form that
CC includes additional features such as cognitive dysfunction, learning
CC disabilities, peripheral sensorimotor neuropathy, urinary sphincter
CC problems, and/or cerebellar atrophy. SPG30 is characterized by onset in
CC the first or second decades of unsteady spastic gait and hyperreflexia
CC of the lower limbs. Inheritance can be autosomal dominant or autosomal
CC recessive. {ECO:0000269|PubMed:21487076, ECO:0000269|PubMed:22258533,
CC ECO:0000269|PubMed:25265257, ECO:0000269|PubMed:25585697,
CC ECO:0000269|PubMed:26125038, ECO:0000269|PubMed:26410750,
CC ECO:0000269|PubMed:28832565, ECO:0000269|PubMed:29159194,
CC ECO:0000269|PubMed:31488895, ECO:0000269|PubMed:32096284}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Neuropathy, hereditary sensory, 2C (HSN2C) [MIM:614213]: A
CC neurodegenerative disorder characterized by onset in the first decade
CC of progressive distal sensory loss leading to ulceration and amputation
CC of the fingers and toes. Affected individuals also develop distal
CC muscle weakness, primarily affecting the lower limbs.
CC {ECO:0000269|PubMed:21820098}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: NESCAV syndrome (NESCAVS) [MIM:614255]: An autosomal dominant
CC neurodegenerative disorder with variable manifestations. Main features
CC are delayed psychomotor development, progressive spasticity,
CC intellectual disability, speech delay, and learning disabilities. Some
CC patients never achieve ambulation. Additional variable features are
CC cortical visual impairment, often associated with optic atrophy, axonal
CC peripheral neuropathy, seizures, dysautonomia, ataxia, and dystonia.
CC Brain imaging often shows progressive cerebellar atrophy and thin
CC corpus callosum. Disease onset is in infancy or early childhood.
CC {ECO:0000269|PubMed:21376300, ECO:0000269|PubMed:25265257,
CC ECO:0000269|PubMed:26125038, ECO:0000269|PubMed:26354034,
CC ECO:0000269|PubMed:27034427, ECO:0000269|PubMed:31805580,
CC ECO:0000269|PubMed:32096284}. 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. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB97363.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE06111.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE06111.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to C-terminal exon with non-canonical splice junction.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X90840; CAA62346.1; -; mRNA.
DR EMBL; AB290172; BAG06726.1; -; mRNA.
DR EMBL; AC011298; AAX93239.1; -; Genomic_DNA.
DR EMBL; AC112784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064906; AAH64906.1; -; mRNA.
DR EMBL; BC111780; AAI11781.1; -; mRNA.
DR EMBL; BC111799; AAI11800.1; -; mRNA.
DR EMBL; AB210029; BAE06111.1; ALT_SEQ; mRNA.
DR EMBL; AF004425; AAD02917.1; -; mRNA.
DR EMBL; AB209138; BAD92375.1; -; mRNA.
DR EMBL; U37194; AAA80352.1; -; mRNA.
DR EMBL; L79946; AAB04640.1; -; mRNA.
DR EMBL; AF038173; AAB97363.1; ALT_INIT; mRNA.
DR EMBL; BX537556; CAH56161.1; -; mRNA.
DR CCDS; CCDS46561.1; -. [Q12756-1]
DR CCDS; CCDS58757.1; -. [Q12756-3]
DR RefSeq; NP_001230937.1; NM_001244008.1. [Q12756-3]
DR RefSeq; NP_001307634.1; NM_001320705.1.
DR RefSeq; NP_004312.2; NM_004321.7. [Q12756-1]
DR RefSeq; XP_016859880.1; XM_017004391.1.
DR PDB; 4EGX; X-ray; 2.51 A; A/B/C/D=430-607.
DR PDB; 4EJQ; X-ray; 1.89 A; A/B/C/D/E/F/G/H=458-607.
DR PDB; 4UXO; EM; 6.30 A; C=1-361.
DR PDB; 4UXP; EM; 6.30 A; C=1-361.
DR PDB; 4UXR; EM; 7.00 A; C=1-361.
DR PDB; 4UXS; EM; 7.00 A; C=1-361.
DR PDBsum; 4EGX; -.
DR PDBsum; 4EJQ; -.
DR PDBsum; 4UXO; -.
DR PDBsum; 4UXP; -.
DR PDBsum; 4UXR; -.
DR PDBsum; 4UXS; -.
DR AlphaFoldDB; Q12756; -.
DR SMR; Q12756; -.
DR BioGRID; 107029; 80.
DR DIP; DIP-42405N; -.
DR IntAct; Q12756; 48.
DR MINT; Q12756; -.
DR STRING; 9606.ENSP00000438388; -.
DR ChEMBL; CHEMBL3308914; -.
DR DrugBank; DB03909; Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR iPTMnet; Q12756; -.
DR PhosphoSitePlus; Q12756; -.
DR SwissPalm; Q12756; -.
DR BioMuta; KIF1A; -.
DR DMDM; 119364606; -.
DR EPD; Q12756; -.
DR jPOST; Q12756; -.
DR MassIVE; Q12756; -.
DR MaxQB; Q12756; -.
DR PaxDb; Q12756; -.
DR PeptideAtlas; Q12756; -.
DR PRIDE; Q12756; -.
DR ProteomicsDB; 25224; -.
DR ProteomicsDB; 58905; -. [Q12756-1]
DR ProteomicsDB; 58906; -. [Q12756-2]
DR Antibodypedia; 1377; 48 antibodies from 17 providers.
DR DNASU; 547; -.
DR Ensembl; ENST00000404283.9; ENSP00000384231.5; ENSG00000130294.18. [Q12756-2]
DR Ensembl; ENST00000498729.9; ENSP00000438388.1; ENSG00000130294.18. [Q12756-3]
DR Ensembl; ENST00000649096.1; ENSP00000497030.1; ENSG00000130294.18. [Q12756-1]
DR Ensembl; ENST00000650053.1; ENSP00000497824.1; ENSG00000130294.18. [Q12756-1]
DR GeneID; 547; -.
DR KEGG; hsa:547; -.
DR MANE-Select; ENST00000498729.9; ENSP00000438388.1; NM_001244008.2; NP_001230937.1. [Q12756-3]
DR UCSC; uc010fzk.3; human. [Q12756-1]
DR CTD; 547; -.
DR DisGeNET; 547; -.
DR GeneCards; KIF1A; -.
DR GeneReviews; KIF1A; -.
DR HGNC; HGNC:888; KIF1A.
DR HPA; ENSG00000130294; Group enriched (brain, pancreas, pituitary gland, retina).
DR MalaCards; KIF1A; -.
DR MIM; 601255; gene.
DR MIM; 610357; phenotype.
DR MIM; 614213; phenotype.
DR MIM; 614255; phenotype.
DR neXtProt; NX_Q12756; -.
DR OpenTargets; ENSG00000130294; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR Orphanet; 101010; Autosomal spastic paraplegia type 30.
DR Orphanet; 970; Hereditary sensory and autonomic neuropathy type 2.
DR Orphanet; 2836; PEHO syndrome.
DR PharmGKB; PA25180; -.
DR VEuPathDB; HostDB:ENSG00000130294; -.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000156474; -.
DR HOGENOM; CLU_001485_10_1_1; -.
DR InParanoid; Q12756; -.
DR OMA; KITICHE; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; Q12756; -.
DR TreeFam; TF105221; -.
DR BRENDA; 5.6.1.3; 2681.
DR PathwayCommons; Q12756; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q12756; -.
DR SIGNOR; Q12756; -.
DR BioGRID-ORCS; 547; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; KIF1A; human.
DR GeneWiki; KIF1A; -.
DR GenomeRNAi; 547; -.
DR Pharos; Q12756; Tbio.
DR PRO; PR:Q12756; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q12756; protein.
DR Bgee; ENSG00000130294; Expressed in right frontal lobe and 148 other tissues.
DR ExpressionAtlas; Q12756; baseline and differential.
DR Genevisible; Q12756; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0098674; C:extrinsic component of neuronal dense core vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0098992; C:neuronal dense core vesicle; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008089; P:anterograde axonal transport; TAS:ProtInc.
DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISS:ARUK-UCL.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0099519; P:dense core granule cytoskeletal transport; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISS:ARUK-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 2.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell projection;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Disease variant;
KW Hereditary spastic paraplegia; Intellectual disability; Membrane;
KW Microtubule; Motor protein; Neurodegeneration; Neuropathy;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..1690
FT /note="Kinesin-like protein KIF1A"
FT /id="PRO_0000125405"
FT DOMAIN 5..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 516..572
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 1575..1673
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1413..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..1558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 366..383
FT /evidence="ECO:0000255"
FT COILED 429..462
FT /evidence="ECO:0000255"
FT COILED 622..681
FT /evidence="ECO:0000255"
FT COILED 801..822
FT /evidence="ECO:0000255"
FT COMPBIAS 1418..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P33173"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P33173"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33173"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33173"
FT MOD_RES 1519
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P33173"
FT MOD_RES 1523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P33173"
FT MOD_RES 1528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33173"
FT MOD_RES 1532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33173"
FT MOD_RES 1548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 394
FT /note="M -> TNTVPGGPKL (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.5"
FT /id="VSP_021853"
FT VAR_SEQ 848
FT /note="R -> RLVGSSAISGCNSYPLLNTCMSERMAALTPSPTFSSPDSDATEPAEE
FT QSVGEEEEEEEEEEDEEEEDLEDDVFPEHALCDGRDPFYDRPPLFS (in isoform
FT 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.5"
FT /id="VSP_021854"
FT VAR_SEQ 1234
FT /note="D -> DRVSLGNDT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_021855"
FT VARIANT 11
FT /note="R -> Q (in SPG30)"
FT /evidence="ECO:0000269|PubMed:32096284"
FT /id="VAR_083686"
FT VARIANT 11
FT /note="R -> W (in SPG30)"
FT /evidence="ECO:0000269|PubMed:28832565"
FT /id="VAR_083687"
FT VARIANT 30
FT /note="M -> T (in SPG30; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083688"
FT VARIANT 46
FT /note="T -> M (in dbSNP:rs182395595)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075471"
FT VARIANT 56
FT /note="Y -> C (in SPG30; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083689"
FT VARIANT 58
FT /note="S -> L (in NESCAVS; dbSNP:rs672601362)"
FT /evidence="ECO:0000269|PubMed:25265257"
FT /id="VAR_075472"
FT VARIANT 69
FT /note="S -> L (in SPG30; dbSNP:rs786200949)"
FT /evidence="ECO:0000269|PubMed:25585697,
FT ECO:0000269|PubMed:26410750, ECO:0000269|PubMed:29159194,
FT ECO:0000269|PubMed:31488895, ECO:0000269|PubMed:32096284"
FT /id="VAR_077467"
FT VARIANT 74
FT /note="Y -> C (in SPG30; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083690"
FT VARIANT 78
FT /note="G -> S (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083691"
FT VARIANT 99
FT /note="T -> M (in NESCAVS; affects the subcellular location
FT of the protein; there is a reduced distal localization and
FT increased accumulation throughout the cell body and
FT proximal neurites in cells transfected with a mutant
FT protein; disrupts microtubule motility; dbSNP:rs387906799)"
FT /evidence="ECO:0000269|PubMed:21376300,
FT ECO:0000269|PubMed:25265257, ECO:0000269|PubMed:26125038"
FT /id="VAR_066649"
FT VARIANT 102
FT /note="G -> D (in NESCAVS; dbSNP:rs672601363)"
FT /evidence="ECO:0000269|PubMed:25265257"
FT /id="VAR_075473"
FT VARIANT 102
FT /note="G -> S (in SPG30; dbSNP:rs1064795534)"
FT /evidence="ECO:0000269|PubMed:26410750"
FT /id="VAR_077468"
FT VARIANT 106
FT /note="T -> N (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083692"
FT VARIANT 136
FT /note="D -> N (in dbSNP:rs374178011)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075474"
FT VARIANT 144
FT /note="V -> F (in NESCAVS; dbSNP:rs672601364)"
FT /evidence="ECO:0000269|PubMed:25265257"
FT /id="VAR_075475"
FT VARIANT 148
FT /note="E -> D (in NESCAVS)"
FT /evidence="ECO:0000269|PubMed:26354034"
FT /id="VAR_083693"
FT VARIANT 167
FT /note="R -> C (in NESCAVS and SPG30; dbSNP:rs672601365)"
FT /evidence="ECO:0000269|PubMed:25265257,
FT ECO:0000269|PubMed:26410750"
FT /id="VAR_075476"
FT VARIANT 167
FT /note="R -> H (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083694"
FT VARIANT 173
FT /note="L -> P (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083695"
FT VARIANT 186
FT /note="V -> F (in NESCAVS)"
FT /evidence="ECO:0000269|PubMed:32096284"
FT /id="VAR_083696"
FT VARIANT 187
FT /note="T -> I (in dbSNP:rs370623844)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075477"
FT VARIANT 199
FT /note="G -> R (in NESCAVS)"
FT /evidence="ECO:0000269|PubMed:27034427"
FT /id="VAR_083697"
FT VARIANT 202
FT /note="A -> P (in NESCAVS; reduces accumulation in distal
FT regions of the neurites; dbSNP:rs672601366)"
FT /evidence="ECO:0000269|PubMed:25265257"
FT /id="VAR_075478"
FT VARIANT 205
FT /note="V -> M (in dbSNP:rs371039513)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075479"
FT VARIANT 215
FT /note="S -> R (in NESCAVS; reduces accumulation in distal
FT regions of the neurites; dbSNP:rs672601367)"
FT /evidence="ECO:0000269|PubMed:25265257"
FT /id="VAR_075480"
FT VARIANT 216
FT /note="R -> C (in NESCAVS; disrupts microtubule motility;
FT dbSNP:rs797045164)"
FT /evidence="ECO:0000269|PubMed:26125038,
FT ECO:0000269|PubMed:31805580"
FT /id="VAR_075481"
FT VARIANT 216
FT /note="R -> H (in NESCAVS; dbSNP:rs672601368)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075482"
FT VARIANT 216
FT /note="R -> P (in NESCAVS; reduces accumulation in distal
FT regions of the neurites; dbSNP:rs672601368)"
FT /evidence="ECO:0000269|PubMed:25265257"
FT /id="VAR_075483"
FT VARIANT 220
FT /note="V -> I (no effect on microtubule motility;
FT dbSNP:rs201314877)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075484"
FT VARIANT 233
FT /note="E -> D (in dbSNP:rs373882732)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075485"
FT VARIANT 249
FT /note="L -> Q (in NESCAVS; dbSNP:rs672601371)"
FT /evidence="ECO:0000269|PubMed:25265257"
FT /id="VAR_075486"
FT VARIANT 252
FT /note="S -> R (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083698"
FT VARIANT 253
FT /note="E -> K (in NESCAVS; reduces accumulation in distal
FT regions of the neurites; disrupts microtubule motility;
FT dbSNP:rs672601369)"
FT /evidence="ECO:0000269|PubMed:25265257,
FT ECO:0000269|PubMed:26125038, ECO:0000269|PubMed:32096284"
FT /id="VAR_075487"
FT VARIANT 254
FT /note="R -> Q (in NESCAVS)"
FT /evidence="ECO:0000269|PubMed:26354034"
FT /id="VAR_083699"
FT VARIANT 254
FT /note="R -> W (in NESCAVS)"
FT /evidence="ECO:0000269|PubMed:26354034,
FT ECO:0000269|PubMed:32096284"
FT /id="VAR_083700"
FT VARIANT 255
FT /note="A -> V (in SPG30; reduces accumulation in distal
FT regions of the neurites; no effect on microtubule motility;
FT dbSNP:rs387906798)"
FT /evidence="ECO:0000269|PubMed:21487076,
FT ECO:0000269|PubMed:22258533, ECO:0000269|PubMed:25265257,
FT ECO:0000269|PubMed:26125038"
FT /id="VAR_066650"
FT VARIANT 258
FT /note="T -> M (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083701"
FT VARIANT 307
FT /note="R -> P (in NESCAVS)"
FT /evidence="ECO:0000269|PubMed:32096284"
FT /id="VAR_083702"
FT VARIANT 307
FT /note="R -> Q (in NESCAVS)"
FT /evidence="ECO:0000269|PubMed:26354034,
FT ECO:0000269|PubMed:27034427"
FT /id="VAR_083703"
FT VARIANT 316
FT /note="R -> W (in NESCAVS; dbSNP:rs672601370)"
FT /evidence="ECO:0000269|PubMed:25265257,
FT ECO:0000269|PubMed:26125038, ECO:0000269|PubMed:26354034"
FT /id="VAR_075488"
FT VARIANT 323
FT /note="S -> P (in NESCAVS)"
FT /evidence="ECO:0000269|PubMed:32096284"
FT /id="VAR_083704"
FT VARIANT 336
FT /note="I -> V (in dbSNP:rs375423065)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075489"
FT VARIANT 350
FT /note="R -> G (in SPG30; reduces accumulation in distal
FT regions of the neurites; dbSNP:rs387907259)"
FT /evidence="ECO:0000269|PubMed:22258533,
FT ECO:0000269|PubMed:25265257"
FT /id="VAR_075490"
FT VARIANT 350
FT /note="R -> W (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083705"
FT VARIANT 355
FT /note="R -> H (in dbSNP:rs373042822)"
FT /evidence="ECO:0000269|PubMed:26125038"
FT /id="VAR_075491"
FT VARIANT 380
FT /note="R -> W (in NESCAVS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31805580"
FT /id="VAR_083706"
FT VARIANT 460
FT /note="A -> G (in SPG30; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083707"
FT VARIANT 623..1690
FT /note="Missing (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083708"
FT VARIANT 843
FT /note="R -> C (in SPG30; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083709"
FT VARIANT 859
FT /note="N -> K (in SPG30; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083710"
FT VARIANT 1026
FT /note="I -> T (in SPG30; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26410750"
FT /id="VAR_077469"
FT VARIANT 1325..1690
FT /note="Missing (in SPG30)"
FT /evidence="ECO:0000269|PubMed:31488895"
FT /id="VAR_083711"
FT CONFLICT 104
FT /note="S -> T (in Ref. 6; AAD02917)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="N -> T (in Ref. 1; CAA62346)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="T -> K (in Ref. 1; CAA62346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="D -> E (in Ref. 8; AAA80352)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="S -> C (in Ref. 8; AAA80352)"
FT /evidence="ECO:0000305"
FT CONFLICT 1108
FT /note="P -> L (in Ref. 2; BAG06726 and 7; BAD92375)"
FT /evidence="ECO:0000305"
FT CONFLICT 1225
FT /note="S -> A (in Ref. 1; CAA62346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1232
FT /note="Q -> H (in Ref. 1; CAA62346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1245
FT /note="D -> N (in Ref. 1; CAA62346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1257
FT /note="V -> I (in Ref. 1; CAA62346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1684
FT /note="R -> W (in Ref. 4; AAI11781)"
FT /evidence="ECO:0000305"
FT HELIX 458..471
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:4EGX"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 538..546
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 554..559
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 583..586
FT /evidence="ECO:0007829|PDB:4EJQ"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:4EJQ"
FT STRAND 590..595
FT /evidence="ECO:0007829|PDB:4EJQ"
FT HELIX 597..604
FT /evidence="ECO:0007829|PDB:4EJQ"
SQ SEQUENCE 1690 AA; 191064 MW; FB3CA33B7060AF60 CRC64;
MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKETPKSF SFDYSYWSHT
SPEDINYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEKDQQGIIP
QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETNITTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAVI
NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD ITDMTNALVG MSPSSSLSAL SSRAASVSSL
HERILFAPGS EEAIERLKET EKIIAELNET WEEKLRRTEA IRMEREALLA EMGVAMREDG
GTLGVFSPKK TPHLVNLNED PLMSECLLYY IKDGITRVGR EDGERRQDIV LSGHFIKEEH
CVFRSDSRGG SEAVVTLEPC EGADTYVNGK KVTEPSILRS GNRIIMGKSH VFRFNHPEQA
RQERERTPCA ETPAEPVDWA FAQRELLEKQ GIDMKQEMEQ RLQELEDQYR REREEATYLL
EQQRLDYESK LEALQKQMDS RYYPEVNEEE EEPEDEVQWT ERECELALWA FRKWKWYQFT
SLRDLLWGNA IFLKEANAIS VELKKKVQFQ FVLLTDTLYS PLPPDLLPPE AAKDRETRPF
PRTIVAVEVQ DQKNGATHYW TLEKLRQRLD LMREMYDRAA EVPSSVIEDC DNVVTGGDPF
YDRFPWFRLV GRAFVYLSNL LYPVPLVHRV AIVSEKGEVK GFLRVAVQAI SADEEAPDYG
SGVRQSGTAK ISFDDQHFEK FQSESCPVVG MSRSGTSQEE LRIVEGQGQG ADVGPSADEV
NNNTCSAVPP EGLLLDSSEK AALDGPLDAA LDHLRLGNTF TFRVTVLQAS SISAEYADIF
CQFNFIHRHD EAFSTEPLKN TGRGPPLGFY HVQNIAVEVT KSFIEYIKSQ PIVFEVFGHY
QQHPFPPLCK DVLSPLRPSR RHFPRVMPLS KPVPATKLST LTRPCPGPCH CKYDLLVYFE
ICELEANGDY IPAVVDHRGG MPCMGTFLLH QGIQRRITVT LLHETGSHIR WKEVRELVVG
RIRNTPETDE SLIDPNILSL NILSSGYIHP AQDDRTFYQF EAAWDSSMHN SLLLNRVTPY
REKIYMTLSA YIEMENCTQP AVVTKDFCMV FYSRDAKLPA SRSIRNLFGS GSLRASESNR
VTGVYELSLC HVADAGSPGM QRRRRRVLDT SVAYVRGEEN LAGWRPRSDS LILDHQWELE
KLSLLQEVEK TRHYLLLREK LETAQRPVPE ALSPAFSEDS ESHGSSSASS PLSAEGRPSP
LEAPNERQRE LAVKCLRLLT HTFNREYTHS HVCVSASESK LSEMSVTLLR DPSMSPLGVA
TLTPSSTCPS LVEGRYGATD LRTPQPCSRP ASPEPELLPE ADSKKLPSPA RATETDKEPQ
RLLVPDIQEI RVSPIVSKKG YLHFLEPHTS GWARRFVVVR RPYAYMYNSD KDTVERFVLN
LATAQVEYSE DQQAMLKTPN TFAVCTEHRG ILLQAASDKD MHDWLYAFNP LLAGTIRSKL
SRRRSAQMRV
