位置:首页 > 蛋白库 > KI21B_MOUSE
KI21B_MOUSE
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   03-AUG-2022, entry version 156.
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}.
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; 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; 18.
DR   IntAct; Q9QXL1; 4.
DR   STRING; 10090.ENSMUSP00000074661; -.
DR   iPTMnet; Q9QXL1; -.
DR   PhosphoSitePlus; Q9QXL1; -.
DR   EPD; Q9QXL1; -.
DR   jPOST; Q9QXL1; -.
DR   MaxQB; Q9QXL1; -.
DR   PaxDb; Q9QXL1; -.
DR   PRIDE; Q9QXL1; -.
DR   ProteomicsDB; 264753; -.
DR   DNASU; 16565; -.
DR   GeneID; 16565; -.
DR   KEGG; mmu:16565; -.
DR   CTD; 23046; -.
DR   MGI; MGI:109234; Kif21b.
DR   eggNOG; KOG0244; Eukaryota.
DR   InParanoid; Q9QXL1; -.
DR   OrthoDB; 390391at2759; -.
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; 16565; 1 hit in 75 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:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 2.
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   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR24115; PTHR24115; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF52540; SSF52540; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024