ID KI21B_MOUSE Reviewed; 1668 AA.
AC Q9QXL1; E9PUY6; P97424;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Kinesin-like protein KIF21B;
DE AltName: Full=Kinesin-like protein KIF6;
GN Name=Kif21b; Synonyms=Kif6;
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, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10225949; DOI=10.1083/jcb.145.3.469;
RA Marszalek J.R., Weiner J.A., Farlow S.J., Chun J., Goldstein L.S.;
RT "Novel dendritic kinesin sorting identified by different process targeting
RT of two related kinesins: KIF21A and KIF21B.";
RL J. Cell Biol. 145:469-479(1999).
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 [MRNA] OF 100-173.
RC TISSUE=Brain cortex;
RA Honeycutt R.J., McClelland M., Chada K., Welsh J.;
RT "Identifying differentially regulated genes in mouse brain using
RT arbitrarily primed PCR.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 491-504, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580 AND THR-583, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1168; SER-1217 AND THR-1239,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, 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).
RN [7]
RP INTERACTION WITH TRIM3, AND SUBCELLULAR LOCATION.
RX PubMed=24086586; DOI=10.1371/journal.pone.0075603;
RA Labonte D., Thies E., Pechmann Y., Groffen A.J., Verhage M., Smit A.B.,
RA van Kesteren R.E., Kneussel M.;
RT "TRIM3 regulates the motility of the kinesin motor protein KIF21B.";
RL PLoS ONE 8:E75603-E75603(2013).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25172774; DOI=10.1016/j.ejcb.2014.07.007;
RA Labonte D., Thies E., Kneussel M.;
RT "The kinesin KIF21B participates in the cell surface delivery of gamma2
RT subunit-containing GABAA receptors.";
RL Eur. J. Cell Biol. 93:338-346(2014).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF THR-96.
RX PubMed=27117409; DOI=10.1016/j.celrep.2016.03.086;
RA Muhia M., Thies E., Labonte D., Ghiretti A.E., Gromova K.V., Xompero F.,
RA Lappe-Siefke C., Hermans-Borgmeyer I., Kuhl D., Schweizer M., Ohana O.,
RA Schwarz J.R., Holzbaur E.L., Kneussel M.;
RT "The kinesin KIF21B regulates microtubule dynamics and is essential for
RT neuronal morphology, synapse function, and learning and memory.";
RL Cell Rep. 15:968-977(2016).
CC -!- FUNCTION: Plus-end directed microtubule-dependent motor protein which
CC displays processive activity (PubMed:27117409, PubMed:10225949). Is
CC involved in regulation of microtubule dynamics, synapse function and
CC neuronal morphology, including dendritic tree branching and spine
CC formation (PubMed:27117409). Plays a role in lerning and memory
CC (PubMed:27117409). Involved in delivery of gamma-aminobutyric acid
CC (GABA(A)) receptor to cell surface (PubMed:25172774).
CC {ECO:0000269|PubMed:10225949, ECO:0000269|PubMed:25172774,
CC ECO:0000269|PubMed:27117409}.
CC -!- SUBUNIT: Interacts with TRIM3; the interaction positively affects
CC motility of KIF21B (PubMed:24086586). Interacts with GABARAP and
CC GABA(A) receptor subunits: GABRG2, GABRA1 and GABRA2 (By similarity).
CC May interact with GABA(A) receptor subunits: GABRB2 and GABRB3 (By
CC similarity). {ECO:0000250|UniProtKB:F1M5N7,
CC ECO:0000269|PubMed:24086586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10225949}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10225949, ECO:0000269|PubMed:24086586,
CC ECO:0000269|PubMed:25172774, ECO:0000269|PubMed:27117409}. Cell
CC projection, growth cone {ECO:0000269|PubMed:24086586}. Cell projection,
CC axon {ECO:0000269|PubMed:10225949}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:F1M5N7}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:27117409, PubMed:25172774). Expressed in spleen and at lower
CC levels in testes (PubMed:10225949). {ECO:0000269|PubMed:10225949,
CC ECO:0000269|PubMed:25172774, ECO:0000269|PubMed:27117409}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice exhibit behavioral changes involving
CC learning and memory deficits. {ECO:0000269|PubMed:27117409}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AF202893; AAF17084.1; -; mRNA.
DR EMBL; AC124550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U71298; AAB39695.1; -; mRNA.
DR RefSeq; NP_001034561.1; NM_001039472.1.
DR AlphaFoldDB; Q9QXL1; -.
DR SMR; Q9QXL1; -.
DR BioGRID; 200940; 19.
DR IntAct; Q9QXL1; 4.
DR STRING; 10090.ENSMUSP00000074661; -.
DR GlyGen; Q9QXL1; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9QXL1; -.
DR PhosphoSitePlus; Q9QXL1; -.
DR EPD; Q9QXL1; -.
DR jPOST; Q9QXL1; -.
DR MaxQB; Q9QXL1; -.
DR PaxDb; 10090-ENSMUSP00000074661; -.
DR ProteomicsDB; 264753; -.
DR DNASU; 16565; -.
DR GeneID; 16565; -.
DR KEGG; mmu:16565; -.
DR AGR; MGI:109234; -.
DR CTD; 23046; -.
DR MGI; MGI:109234; Kif21b.
DR eggNOG; KOG0244; Eukaryota.
DR InParanoid; Q9QXL1; -.
DR OrthoDB; 1131899at2759; -.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16565; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Kif21b; mouse.
DR PRO; PR:Q9QXL1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXL1; Protein.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
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: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; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0022038; P:corpus callosum development; IMP:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd01372; KISc_KIF4; 1.
DR CDD; cd22262; Rcc_KIF21B; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF28; KINESIN-LIKE PROTEIN KIF21B ISOFORM X1; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Direct protein sequencing; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1668
FT /note="Kinesin-like protein KIF21B"
FT /id="PRO_0000125465"
FT DOMAIN 8..371
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 1308..1345
FT /note="WD 1"
FT REPEAT 1348..1386
FT /note="WD 2"
FT REPEAT 1412..1450
FT /note="WD 3"
FT REPEAT 1453..1495
FT /note="WD 4"
FT REPEAT 1504..1541
FT /note="WD 5"
FT REPEAT 1545..1584
FT /note="WD 6"
FT REPEAT 1587..1624
FT /note="WD 7"
FT REGION 401..1100
FT /note="Interaction with TRIM3"
FT /evidence="ECO:0000269|PubMed:24086586"
FT REGION 553..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 372..465
FT /evidence="ECO:0000255"
FT COILED 924..1019
FT /evidence="ECO:0000255"
FT COMPBIAS 553..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..624
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 1150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75037"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1239
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75037"
FT MUTAGEN 96
FT /note="T->N: Abolishes processive activity."
FT /evidence="ECO:0000269|PubMed:27117409"
FT CONFLICT 1276
FT /note="S -> A (in Ref. 1; AAF17084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1668 AA; 186180 MW; 99691F966387A577 CRC64;
MAGQGDCCVK VAVRIRPQLS KEKIEGCHIC TSVTPGEPQV LLGKDKAFTY DFVFDLDTWQ
EQIYSTCVSK LIEGCFEGYN ATVLAYGQTG AGKTYTMGTG FDTVTSEEEQ GIIPRAIAHL
FRGIDERKRR AQEKGVTGPE FKVSAQFLEL YNEEILDLFD STRDPDARHR RSNIKIHEDA
NGGIYTTGVT SRLINSQEEL IQCLKQGALS RTTASTQMNV QSSRSHAIFT IHLCQMRVCA
QPDLVNETVT GLPDGAAPTG TEYETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
LLALGNVISA LGDQSKKVVH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
TLKYANRARN IKNKVVVNQD KTSQQISALR AEIARLQMEL MEYKAGKRVI GEDGTEGYSD
LFRENAMLQK ENGALRLRVK AMQEAIDAIN NRVTQLMSQE ANLLLAKAGD GNEAIGALIQ
NYIREIEELR TKLLESEAMN ESLRRSLSRA SARNPYSLGA SPAGPAFGGS PATSMEDASE
VIRKAKQDLE RLKKKEVRQR RKSPEKEAFK KRAKLQAENS EETDENEAEE EEEERDESGC
EEEEGREDED EDSGSEESLV DSDSDPEEKE VNFQADLADL TCEIEIKQKL IDELENSQRR
LQTLKHQYEE KLILLQNKIR DTQLERDRVL QNLSTMECYT EEKANKIKAD YEKRLREMNR
DLQKLQAAQK EHARLLKNQS RYERELKKLQ AEVAEMKKAK VALMKQMREE QQRRRLVETK
RNREIAQLKK EQRRQEFQIR ALESQKRQQE IVLRRKTQEV SALRRLAKPM SERVAGRVGL
KPPNMDSGAE VSASTTSSEA ESGARSVSSI VRQWNRKIDH FLGDRPTATV NGGRPARKKF
QKKGASQSFS KAARLKWQSL ERRIIDIVMQ RMTIVNLEAD MERLIKKREE LFLLQEALRR
KREHLQAESP EEEKGLQELA EEIEVLAANI DYINDSITDC QATIVQLEET KEELDSTDTS
VVISSCSLAE ARLLLDNFLK ASIDKGLQVA QKEAQIRLLE GRLRQTDMTG SSQNHLLLDA
LREKAEAHPE LQALIYNVQH ENGYASTDEE VSEFSEGSFS QSFTMKGSTS HDDFKFKGEP
KLSAQMKAVS AECLGPPLDS STKNITKSLA SLVEIKEDGV GFSIRDPYYR DKVSRTVSLP
TRGSTFPRQS RGATDTSPLT RRKSYDRGQP IRSTDMGFTP PSSPPTRPRN DRNVFSRLTS
NQSQGSALDK SDDSDSSLSE VLRGIITPIG GAKGARTAPL QCISMAEGHT KPILCLDATD
ELLFTGSKDR SCKMWNLVTG QEIAALKGHP NNVVSIKYCS HSGLVFSVSS SYIKVWDIRD
SAKCIRTLTS SGQVISGDAC IATSTRAITS AQGEHQINQM ALSPSGSMLY VASGNAVRIW
ELNRFQPIGK LTGHIGPVMC LTVTQTSNQH DLVVTGSKDH YVKMFQLGDC VTGTIGPTHN
FEPPHYDGIE CLAIQGDILF SGSRDNGIKK WDLDQQELIQ QIPNAHKDWV CALAFVPGRP
MLLSACRAGF IKVWNVDNFT PIGEIKGHDS PINAICTNSK HIFTASSDCR VKLWNYVPGL
TPCLPRRVLA IKGRAPPCPD LPPPPLTLPI LPFPVFPPPR SELLLHVT
//
