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Database: UniProt
Entry: A0A2Y9M684_DELLE
LinkDB: A0A2Y9M684_DELLE
Original site: A0A2Y9M684_DELLE 
ID   A0A2Y9M684_DELLE        Unreviewed;      1655 AA.
AC   A0A2Y9M684;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Kinesin-like protein KIF21B isoform X2 {ECO:0000313|RefSeq:XP_022417649.1};
GN   Name=KIF21B {ECO:0000313|RefSeq:XP_022417649.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022417649.1};
RN   [1] {ECO:0000313|RefSeq:XP_022417649.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022417649.1};
RG   RefSeq;
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   RefSeq; XP_022417649.1; XM_022561941.1.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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; 6.
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:UP000248483};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          67..429
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REPEAT          1336..1375
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1532..1571
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1573..1614
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1615..1645
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          563..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1242..1296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..464
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          681..863
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          971..1040
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        604..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..668
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..910
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1242..1261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         146..153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1655 AA;  184733 MW;  F12A0FE173FEA315 CRC64;
     MSCAWWRWAQ AHSRKWRRLD LDPGHPCFQA RAPHPAPRGL VIRLLIRSFW APPCLRFLQP
     FPHVMAVTTN AGRIRPQLSK EKIEGCHICT SVTPGEPQVL LGKDKAFTYD FVFDLDTWQE
     QIYSTCVSRL VEGCFEGYNA TVLAYGQTGA GKTYTMGTGF DVAMAEEEQG IIPRAIAHLF
     GGIAERKRRA QEQGVAGPEF KVSAQFLELY NEEILDLFDS ARDPDARHRR SNIKIHEDAN
     GGIYTTGVTS RLISSQEELI QCLKQGALSR TTASTQMNVQ SSRSHAIFTI HVCQMRLCTR
     PDLVNEAVTG LPDGTAPSGE YETLTAKFHF VDLAGSERLK RTGATGERAK EGISINCGLL
     ALGNVISALG DQSKKVVHVP YRDSKLTRLL QDSLGGNSQT IMIACVSPSD RDFMETLNTL
     KYANRARNIK NKVVVNQDKT SQQISALRAE IARLQMELME YKAGKRVIGE DGAEGYSDLF
     RENAMLQKEN GALRLRVKAM QEAIDAINSR VTQLMSQEAN LLLAKAGDGS EAIGALIQNY
     IREIEDLRTK LLESEAMNES LRRSLSRAST RGPYSLGASP VVPTGSMEDA AEVIRRAKQD
     LERLKKKEVR QRRKSPEKEA FKKRAKLQQE NSEETDDNEA EEEDEEPEES GREDEDSGSE
     ESLVDSDSDP EDKEVNYQAD LADLTCEIEI KQKLIDELEN SQRRLQTLKH QYEEKLILLQ
     NKIRDTQLER DRVLQNLSTM ECYTEEKANK IKADYEKRLR EMNRDLQKLQ AAQKEHARLL
     KNQSRYEREL KKLQAEVAEM KKAKVALMKQ MREEQHRRRL AETKRNREIA QLKKEQRRQE
     FQIRALESQK RQQEMVLRRK TQEVSALRRL AKPMSERVAG RVGPKSPMLD SGAEVSASTT
     SSEAESGARS VSSIVRQWDH KISHFLENHP MPTVSGARPA RKKFQKKGAS QSFSKAARLK
     WQSLERRIVD IVMQRMAIAN LEADMERLIK KREELSLLQE ALRRKRERLQ AESPEEEKGL
     QELAEEIEVL AANIDYINDS IGDCQATIVQ LEETKEELDS TDTSVVISSC SLAEARLLLD
     NFLKASIDKG LQVAQKEAQI RLLEGRLRQT DIAGPSQNHL LLDALREKAE AHPELQALIH
     NVQQENGYAS TDEEVSEFSE GSFSQSFTMK GSTSHDDFKF KGEPKLSAQM KAVSAECLGP
     PLDVSTKNIT KSLASLVEIK EDGVGFSIRD PYYRDKVSRT ISLPSRGSTF PRQSRGAETS
     PLTRRKSYDR GQPIRSTDVG FTPPSSPPTR PRNDRNVFSR LTSNQSQGSA LDKGIITPVG
     GARGARTAPL QCVSMAEGHT KPILCLDATD ELLFTGSKDR SCKMWNLVTG QEIAALKGHP
     SNVVSIKYCS LSGLVFSVST SYIKVWDIRD SAKCVRTLTS SGQVVSGDAC AAASTRTITS
     AQGEHQINQI ALSPSGSMLY AASGNAVRIW ELNRFQPVGK LTGHIGPVMC LTVAQTASQH
     DLVVTGSKDH YVKMFQLGEC VTGTVGPTHN FEPPHYDGIE CLAIQGDVLF SGSRDNGIKK
     WDLAQQELMQ QIPTAHKDWV CALAFVPGRP MLLSACRAGV IKVWNVDNFT PIGEIKGHDS
     PINAMCTNAR HIFSASSDLT VKFWSARRLV PSGPH
//
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