KI26A_MOUSE
ID KI26A_MOUSE Reviewed; 1881 AA.
AC Q52KG5; C9EF47; Q6PCY3; Q6ZPV4; Q99PT4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Kinesin-like protein KIF26A;
GN Name=Kif26a; Synonyms=Kiaa1236;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, MICROTUBULE-BINDING, LACK OF ATPASE
RP ACTIVITY, AND INTERACTION WITH GRB2.
RC STRAIN=A/J;
RX PubMed=19914172; DOI=10.1016/j.cell.2009.10.023;
RA Zhou R., Niwa S., Homma N., Takei Y., Hirokawa N.;
RT "KIF26A is an unconventional kinesin and regulates GDNF-Ret signaling in
RT enteric neuronal development.";
RL Cell 139:802-813(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 467-613.
RX PubMed=11416179; DOI=10.1073/pnas.111145398;
RA Miki H., Setou M., Kaneshiro K.;
RT "All kinesin superfamily protein, KIF, genes in mouse and human.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7004-7011(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-1881.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 781-1881.
RC STRAIN=C57BL/6J; 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Atypical kinesin that plays a key role in enteric neuron
CC development. Acts by repressing a cell growth signaling pathway in the
CC enteric nervous system development, possibly via its interaction with
CC GRB2 that prevents GRB2-binding to SHC, thereby attenating the GDNF-Ret
CC signaling. Binds to microtubules but lacks microtubule-based motility
CC due to the absence of ATPase activity. {ECO:0000269|PubMed:19914172}.
CC -!- SUBUNIT: Interacts with GRB2 (via SH2 domain).
CC {ECO:0000269|PubMed:19914172}.
CC -!- INTERACTION:
CC Q52KG5; Q60631: Grb2; NbExp=2; IntAct=EBI-2480646, EBI-1688;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in several neuronal populations.
CC {ECO:0000269|PubMed:19914172}.
CC -!- DEVELOPMENTAL STAGE: Strong expression is detected in substantia nigra
CC in brain and enteric nervous system in colon at P12. In colon sections
CC at 12.5 dpc, 14.5 dpc, and P12, it is exclusively expressed in enteric
CC nervous system (ENS). Also detected in dorsal root ganglion and spinal
CC cord gray matter at 14.5 dpc. {ECO:0000269|PubMed:19914172}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit growth retardation, become
CC emaciated, and die within 5 weeks of birth. The median and mean life
CC span is 15 and 16 days. Macroscopic dissection reveal that mice
CC suffered from megacolon, with dilation from the distal small intestine
CC to the proximal colon and display enteric nerve hyperplasia. Severe
CC occlusion are observed in the distal colon, because the colon motility
CC is not coordinated. Defects are due to abnormal enteric nervous system
CC (ENS) proliferation. {ECO:0000269|PubMed:19914172}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIF26 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- CAUTION: In contrast to other kinesin-like proteins, residues required
CC for ATPase activity are missing. {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; GQ489027; ACV92100.1; -; mRNA.
DR EMBL; AC112520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB054031; BAB32495.1; -; Genomic_DNA.
DR EMBL; AK129315; BAC98125.1; -; mRNA.
DR EMBL; BC059062; AAH59062.1; -; mRNA.
DR EMBL; BC094358; AAH94358.1; -; mRNA.
DR CCDS; CCDS49186.1; -.
DR RefSeq; NP_001091090.1; NM_001097621.1.
DR AlphaFoldDB; Q52KG5; -.
DR SMR; Q52KG5; -.
DR IntAct; Q52KG5; 2.
DR STRING; 10090.ENSMUSP00000119482; -.
DR iPTMnet; Q52KG5; -.
DR PhosphoSitePlus; Q52KG5; -.
DR jPOST; Q52KG5; -.
DR PaxDb; Q52KG5; -.
DR PRIDE; Q52KG5; -.
DR ProteomicsDB; 264754; -.
DR Antibodypedia; 28168; 85 antibodies from 14 providers.
DR Ensembl; ENSMUST00000128402; ENSMUSP00000119482; ENSMUSG00000021294.
DR GeneID; 668303; -.
DR KEGG; mmu:668303; -.
DR UCSC; uc007pem.1; mouse.
DR CTD; 26153; -.
DR MGI; MGI:2447072; Kif26a.
DR VEuPathDB; HostDB:ENSMUSG00000021294; -.
DR eggNOG; KOG4280; Eukaryota.
DR GeneTree; ENSGT00940000159075; -.
DR HOGENOM; CLU_002423_0_0_1; -.
DR InParanoid; Q52KG5; -.
DR OMA; GECDAQA; -.
DR OrthoDB; 29955at2759; -.
DR PhylomeDB; Q52KG5; -.
DR TreeFam; TF105235; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 668303; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Kif26a; mouse.
DR PRO; PR:Q52KG5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q52KG5; protein.
DR Bgee; ENSMUSG00000021294; Expressed in rostral migratory stream and 147 other tissues.
DR Genevisible; Q52KG5; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0048484; P:enteric nervous system development; IMP:UniProtKB.
DR GO; GO:0009968; P:negative regulation of signal transduction; IMP:UniProtKB.
DR GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; IMP:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1881
FT /note="Kinesin-like protein KIF26A"
FT /id="PRO_0000307300"
FT DOMAIN 364..718
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 20..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1652..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1780..1812
FT /evidence="ECO:0000255"
FT COMPBIAS 939..954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 462..469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULI4"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULI4"
FT MOD_RES 1654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULI4"
FT CONFLICT 120
FT /note="T -> A (in Ref. 1; ACV92100)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="N -> D (in Ref. 1; ACV92100)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> P (in Ref. 1; ACV92100)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="V -> I (in Ref. 4; BAC98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="T -> I (in Ref. 4; BAC98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1101
FT /note="G -> S (in Ref. 4; BAC98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118
FT /note="L -> F (in Ref. 5; AAH94358)"
FT /evidence="ECO:0000305"
FT CONFLICT 1200
FT /note="A -> V (in Ref. 4; BAC98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1312
FT /note="T -> S (in Ref. 1; ACV92100)"
FT /evidence="ECO:0000305"
FT CONFLICT 1333
FT /note="T -> N (in Ref. 4; BAC98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1421
FT /note="V -> A (in Ref. 4; BAC98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1437
FT /note="L -> P (in Ref. 1; ACV92100)"
FT /evidence="ECO:0000305"
FT CONFLICT 1518
FT /note="T -> TA (in Ref. 4; BAC98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1577
FT /note="S -> P (in Ref. 1; ACV92100)"
FT /evidence="ECO:0000305"
FT CONFLICT 1769
FT /note="A -> V (in Ref. 4; BAC98125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1773
FT /note="P -> S (in Ref. 1; ACV92100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1881 AA; 196313 MW; 6A8B5235D7DB70D2 CRC64;
MVGRGASLCA VQPAVAECGP ARETPPLEVS PRKRLPAGLD QDPCSSRPAP EGAGASAEQS
HSAGGGGWCR HCHTKLVELK RQAWKLVSGP GTPLRDPCLS TLLLDKLPAS GVQPACRPDT
ESRCDVCTTH LHQLTREALR LLQTPASHED PNASRGGLAA PSSRDPPGPV GLMGRQPPVG
PDRRKATAWP PGPSVQVSVA PAGLGGALST VTIQAQQCLE GVWSLSRVNS FLPPTCLAEA
AVAAVAVADT VRDCAPAAGP ERMSKAWGRG AACTTALVTP APGTSAGGST GPSAAASFFI
RAAQKLSLAS KRKKHHPPPA PSTRGTSTYP TDFSGSLQLW PPPVPPCLLR AASKAKENPS
SFGKVKVMLR IWPAQGVQRS AESTSFLKVD SRKKQVTLYD PAAGPPGCAG LRHAPTAPVP
KMFAFDAIFP QDSEQAEVCS GTVADVLQSV VSGADGCIFS FGHMSLGKSY TMIGKDSSPQ
SLGIVPCAIS WLFRLIDERK ERLGTRFSIR VSAVEVCGHD QSLRDLLAEV ASGSLQDTQS
PGVYLREDPV CGTQLQNQNE LRAPTAEKAA FYLDAALAAR STSRAGCGEE ARRSSHMLFT
LHVYQYRVEK CGQGGMSGGR SRLHLIDLGS CDAAVGRGGE ASGGPLCLSL SALGSVILAL
VNGAKHVPYR DHRLTMLLRE SLATTNCRTT MIAHISDSPA HHAETLSTVQ LAARIHRLRR
KKGKHASSSS GGESSCEEGR ARRPPHLRPF HPRAVVLDPD RSAPGLSGDP DYSSSSEQSC
DTVIYVGPGG MALSDRELTD NEGPPDFVPI IPALSRRRPS EGPRDADHFR CSTFAELQER
LECIDGSEAF PGPQGGSDGA QASPARGGRK PSLPEATPSR KAVAPTVVTS CPRGSPGHDT
HRSASDPSKT GTQSEQRVDG SRPEPPASDK TSGGGGRRPL PSPAPPPPRQ PEAQGIPKEP
GGEGTDSVLR TPPVGMSGQA ALPPLLSDSA YLSPSARGRH LERGLLTTTV TLQQPVELNG
EDELVFTVVE ELPLGGLAGA TRPSSLASMS SDCSLQALAS GSRPVSIISS INDEFDAYTS
QMSEGPGDPG EFPEGTAWAG GSPASSIGSW LSDVGVCLSE SRGPTPQPPF SPNSAAGPGP
PEFPTPGSSL EESKVRSSEC GRPDNPGSAR SLHPGEAVAT TQTQPGREPW ARSPHEVASA
QTIHSSLPRK PRTTSTASRA RPSRGPYSPG GLFEDPWLLR AEDCDTRQIA STGRAPSPTP
GSPRLPETQM MLACAQRVVD GCEVASRMSR RPEAVARIPP LRRGATTLGV TTPAASCGDA
PAEAVVHSGS LKTTSGSKKS VSPKGAFFPR PSGAGPPAPP VRKSSLEQST ALTPTQALGL
TRAGAPSAFR GEEEARPSGR SDSSVPKATS SLKARAGKMD VPYRPSGHMS LERCEGLAHG
SSKVRDVVGR PPRAVPRLGV PSASPPLGPA PACRNSPAKG VGATKPPAGG AKGRNLGPST
SRALGAPVKP LGPVAGKTAG GAVPGPRAAP RAVPGIGAKA GRGTIMGTKQ AFRAAHSRVH
ELAASGSPSR GGLSWGSTDS DSGNDSGVNL AEERQPSSPA LPSPYSKVTA PRRPQRYSSG
HGSDNSSVLS GELPPAMGRT ALFYHSGGSS GYESMIRDSE ATGSASSAPD SMSESGTASL
GARSRSLKSP KKRATGLQRR RLIPAPLPDA AALGRKPSLP GQWVDLPPPL AGSLKEPFEI
KVYEIDDVER LQRHRLPLRE NEAKPSQDAE KGPVCISSKL RLAERRQQRL QEVQAKRDHL
CEELAETQGR LMVEPGRWLE QFEVDPELEP ESAEYLVALE QATAALEQCV NLCKAHVMMV
TCFDIGVAAT TAVPGPQEVD V
