KI21B_RAT
ID KI21B_RAT Reviewed; 1634 AA.
AC F1M5N7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Kinesin-like protein KIF21B {ECO:0000305};
GN Name=Kif21b {ECO:0000312|RGD:1306206};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:EDM09667.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4] {ECO:0000305}
RP INTERACTION WITH GABRG2; GABRA1; GABRA2; GABRB2; GABRB3 AND GABARAP,
RP 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).
CC -!- FUNCTION: Plus-end directed microtubule-dependent motor protein which
CC displays processive activity. Is involved in regulation of microtubule
CC dynamics, synapse function and neuronal morphology, including dendritic
CC tree branching and spine formation. Plays a role in lerning and memory.
CC Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to
CC cell surface. {ECO:0000250|UniProtKB:Q9QXL1}.
CC -!- SUBUNIT: Interacts with TRIM3; the interaction positively affects
CC motility of KIF21B (By similarity). Interacts with GABARAP and GABA(A)
CC receptor subunits: GABRG2, GABRA1 and GABRA2 (PubMed:25172774). May
CC interact with GABA(A) receptor subunits: GABRB2 and GABRB3
CC (PubMed:25172774). {ECO:0000250|UniProtKB:Q9QXL1,
CC ECO:0000269|PubMed:25172774}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9QXL1}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:25172774}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:25172774}.
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; AABR07021001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07021002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473958; EDM09667.1; -; Genomic_DNA.
DR RefSeq; NP_001099460.1; NM_001105990.1.
DR AlphaFoldDB; F1M5N7; -.
DR SMR; F1M5N7; -.
DR STRING; 10116.ENSRNOP00000011324; -.
DR iPTMnet; F1M5N7; -.
DR PhosphoSitePlus; F1M5N7; -.
DR jPOST; F1M5N7; -.
DR PaxDb; F1M5N7; -.
DR PeptideAtlas; F1M5N7; -.
DR PRIDE; F1M5N7; -.
DR Ensembl; ENSRNOT00000011324; ENSRNOP00000011324; ENSRNOG00000008471.
DR GeneID; 289397; -.
DR KEGG; rno:289397; -.
DR CTD; 23046; -.
DR RGD; 1306206; Kif21b.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000159650; -.
DR HOGENOM; CLU_001485_4_5_1; -.
DR InParanoid; F1M5N7; -.
DR OMA; HKQRVIQ; -.
DR OrthoDB; 390391at2759; -.
DR TreeFam; TF105224; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:F1M5N7; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000008471; Expressed in frontal cortex and 17 other tissues.
DR ExpressionAtlas; F1M5N7; baseline and differential.
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; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1634
FT /note="Kinesin-like protein KIF21B"
FT /id="PRO_0000438149"
FT DOMAIN 8..371
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 1303..1340
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 1343..1381
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 1407..1445
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1448..1490
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 1499..1536
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 1540..1579
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 1582..1619
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 401..1095
FT /note="Interaction with TRIM3"
FT /evidence="ECO:0000250|UniProtKB:Q9QXL1"
FT REGION 521..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 924..1012
FT /evidence="ECO:0000255"
FT COMPBIAS 553..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..619
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1214
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:0000250|UniProtKB:Q9QXL1"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXL1"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75037"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75037"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75037"
FT MOD_RES 1234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75037"
SQ SEQUENCE 1634 AA; 182563 MW; 49DAB21E278F0044 CRC64;
MAGQGDCCVK VAVRIRPQLS KEKIEGCHIC TSVTPGEPQV LLGKDKAFTY DFVFDLDTWQ
EQIYSTCVSK LIEGCFEGYN ATVLAYGQTG AGKTYTMGTG FDTVTSEEEQ GIIPRAIAHL
FRGIDERKRR AQEQGVTGPE FKVSAQFLEL YNEEILDLFD STRDPDARHR RSNIKIHEDA
NGGIYTTGVT SRLINSQEEL IQCLKQGALS RTTASTQMNV QSSRSHAIFT IHLCQMRVCA
QPDLVNETVT GLPDGTAPTG TEYETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
LLALGNVISA LGDQSKKVVH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
TLKYANRARN IKNKVVVNQD KTSQQISALR AEIARLQMEL MEYKAGKRVI GEDGAEGYSD
LFRENAMLQK ENGALRLRVK AMQEAIDAIN NRVTQLMSQE ANLLLAKAGD GNEAIGALIQ
NYIREIEELR TKLLESEAMN ESLRRSLSRA SARNPYSLGA SPAGPAFGGS PASSMEDASE
VIRRAKQDLE RLKKKEVRQR RKSPEKEAFK KRAKLQQENS EETDENEAEE EEEERDESGC
EEEEDEDSGS EESLVDSDSD PEEKEVNFQA DLADLTCEIE IKQKLIDELE NSQRRLQTLK
HQYEEKLILL QNKIRDTQLE RDRVLQNLST MECYTEEKAN KIKADYEKRL REMNRDLQKL
QAAQKEHARL LKNQSRYERE LKKLQTEVAE MKKAKVALMK QMREEQQRRR LVETKRNREI
AQLKKEQRRQ EFQIRALESQ KRQQEIVLRR KTQEVSALRR LAKPMSERVA GRVGLKPPNM
DSGAEVSAST TSSEAESGAR SVSSIVRQWN RKINHFLGDH PTATVNGARP ARKKFQKKGA
SQSFSKAARL KWQSLERRII DIVMQRMTIV NLEADMERLI KKREELFLLQ EALRRKRERL
QAESPEEEKG LQELAEEIEV LAANIDYIND SITDCQATIM QLEETKEELD STDTSVVISS
CSLAEARLLL DNFLKASIDK GLQVAQKEAQ IRLLEGRLRQ TDMTGSSQNH LLLDALREKA
EAHPELQALI YNVQHENGYA STDEEVSEFS EGSFSQSFTM KGSTSHDDFK FKGEPKLSAQ
MKAVSAECLG PPLDSSTKNI TKSLASLVEI KEDGVGFSIR DPYYRDKVSR TVSLPTRGST
FPRQSRGATD TSPLTRRKSY DRGQPIRSTD IGFTPPSSPP TRPRNDRNVF SRLTSNQSQG
SALDKSDDSD SSLSEVLRGI ITPIGGAKGA RTAPLQCVSM AEGHTKPILC LDATDELLFT
GSKDRSCKMW NLVTGQEIAA LKGHPNNVVS IKYCSHSGLV FSVSSSYVKV WDIRDSAKCI
RTLTSSGQVI SGDACMATST RAITSSQGEH QINQMALSPS GTMLYVASGN AVRIWELNRF
QPIGKLTGHI GPVMCLTVTQ TSNQHDLVVT GSKDHYVKMF QLGDCVTGTI GPTHNFEPPH
YDGIECLAIQ GDILFSGSRD NGIKKWDLDQ QELIQQIPNA HKDWVCALAF VPGRPMLLSA
CRAGFIKVWN VDNFTPIGEI KGHDSPINAI CTNSKHIFTA SSDCRVKLWN YVPGLTPCLP
RRVLAIKGRA TTLP
