ID G3QFV0_GORGO Unreviewed; 1639 AA.
AC G3QFV0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Kinesin family member 21B {ECO:0000313|Ensembl:ENSGGOP00000001182.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000001182.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000001182.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000001182.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000001182.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; CABD030008267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030008268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9593.ENSGGOP00000001182; -.
DR Ensembl; ENSGGOT00000001206.3; ENSGGOP00000001182.3; ENSGGOG00000001197.3.
DR GeneTree; ENSGT00940000159650; -.
DR InParanoid; G3QFV0; -.
DR OMA; HKQRVIQ; -.
DR Proteomes; UP000001519; Chromosome 1.
DR Bgee; ENSGGOG00000001197; Expressed in prefrontal cortex and 4 other cell types or tissues.
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-UniRule.
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 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; 3.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 1..363
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 1302..1341
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1498..1537
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1539..1580
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1581..1611
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 502..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 371..398
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 431..498
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 628..810
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 925..1008
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 585..615
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1639 AA; 182875 MW; 68BAB2E44D667A60 CRC64;
MCWAKKGIRP QLSKEKIEGC HICTSVTPGE PQVLLGKDKA FTYDFVFDLD TWQEQIYSTC
VSKLIEGCFE GYNATVLAYG QTGAGKTYTM GTGFDMATSE EEQGIIPRAI AHLFGGIAER
KRRAQEQGMA GPEFKVSAQF LELYNEEILD LFDSTRDPDT RHRRSNIKIH EDANGGIYTT
GVTSRLIHSQ EELIQCLKQG ALSRTTASTQ MNVQSSRSHA IFTIHLCQMR MCTQPDLVNE
AVTGLPDGTP PSSEYETLTA KFHFVDLAGS ERLKRTGATG ERAKEGISIN CGLLALGNVI
SALGDQSKKV VHVPYRDSKL TRLLQDSLGG NSQTIMIACV SPSDRDFMET LNTLKYANRA
RNIKNKVVVN QDKTSQQISA LRAEIARLQM ELMEYKAGKR VIGEDGAEGY SDLFRENAML
QKENGALRLR VKAMQEAIDA INNRVTQLMS QEANLLLAKA GDGNEAIGAL IQNYIREIEE
LRTKLLESEA MNESLRRSLS RASARSPYSL GASPAAPAFG GSPASSMEDA SEVIRRAKQD
LERLKKKEVR QRRKRHCVGM RLCFWAPLSE ARPTPMVPGA QEEEERDESG CEEEEGREDE
DEDSGSEESL VDSDSDPEEK EVNFQADLAD LTCEIEIKQK LIDELENSQR RLQTLKHQYE
EKLILLQNKI RDTQLERDRV LQNLSTMECY TEEKANKIKA DYEKRLREMN RDLQKLQAAQ
KEHARLLKNQ SRYERELKKL QAEVAEMKKA KVALMKQMRE EQQRRRLVET KRNREIAQLK
KEQRRQEFQI RALESQKRQQ EMVLRRKTQE VSALRRLAKP MSERVAGRAG LKPPMLDSGA
EVSASTTSSE AESGARSVSS IVRQWNRKIN HFLGDHPAPT VNGTRPARKK FQKKGASQSF
SKAARLKWQS LERRIIDIVM QRMTIVNLEA DMERLIKKRE ELFLLQEALR RKRERLQAES
PEEEKGLQEL AEEIEVLAAN IDYINDSITD CQATIVQLEE TKEELDSTDT SVVISSCSLA
EARLLLDNFL KASIDKGLQV AQKEAQIRLL EGRLRQTDMA GSSQNHLLLD ALREKAEAHP
ELQALIYNVQ QENGYASTDE EISEFSEGSF SQSFTMKGST SHDDFKFKSE PKLSAQMKAV
SAECLGPPLD ISTKNITKSL ASLVEIKEDG VGFSVRDPYY RDRVSRTVSL PTRGSTFPRQ
SRATETSPLT RRKSYDRGQP IRSTDVGFTP PSSPPTRPRN DRNVFSRLTS NQSQGSALDN
LAMVSLADEH AFSPSLPGRG IISPVGGAKG ARTAPLQCVS MAEGHTKPIL CLDATDELLF
TGSKDRSCKM WNLVTGQEIA ALKGHPNNVV SIKYCSHSGL VFSVSTSYIK VWDIRDSAKC
IRTLTSSGQV ISGDACAATS TRAITSAQGE HQINQIALSC SGTMLYAASG NAVRIWELSR
FQPVGKLTGH IGPVMCLTVT QTASQHDLVV TGSKDHYVKM FELGECVTGT IGPTHNFEPP
HYDGIECLAI QGDILFSGSR DNGIKKWDLD QQELIQQIPN AHKDWVCALA FIPGRPMLLS
ACRAGVIKVW NVDNFTPIGE IKGHDSPINA ICTNAKHIFT ASSDCRVKLW NYVPGLTPCL
PRRVLAIKGR ATTLCFLTV
//
