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Database: UniProt
Entry: A0A1L8GM91_XENLA
LinkDB: A0A1L8GM91_XENLA
Original site: A0A1L8GM91_XENLA 
ID   A0A1L8GM91_XENLA        Unreviewed;       730 AA.
AC   A0A1L8GM91;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   Name=kif2c.L {ECO:0000313|RefSeq:XP_018113838.1,
GN   ECO:0000313|Xenbase:XB-GENE-17344777};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018113838.1};
RN   [1] {ECO:0000313|RefSeq:XP_018113838.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018113838.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018113838.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000256|ARBA:ARBA00004629}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC       ECO:0000256|RuleBase:RU000394}.
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DR   RefSeq; XP_018113838.1; XM_018258349.2.
DR   AlphaFoldDB; A0A1L8GM91; -.
DR   STRING; 8355.A0A1L8GM91; -.
DR   PaxDb; 8355-A0A1L8GM91; -.
DR   GeneID; 108714276; -.
DR   KEGG; xla:108714276; -.
DR   AGR; Xenbase:XB-GENE-17344777; -.
DR   CTD; 108714276; -.
DR   Xenbase; XB-GENE-17344777; kif2c.L.
DR   OMA; RTTLECH; -.
DR   OrthoDB; 239968at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 108714276; Expressed in egg cell and 18 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd01367; KISc_KIF2_like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 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   PANTHER; PTHR47971:SF19; KINESIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   BINDING         353..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   730 AA;  82727 MW;  393D069531309654 CRC64;
     MERLLANRLF TGLAVKIMRS NGVIHNANIT SVNMDRSSVN VEWKEGEASK GKEISFADVI
     SVNPELLDAV LVPPNVKENM PTQRIVSSQN HKRKTISKIP APKEVTTKNS TLPECGTQSV
     LRERSTRMTA IHETLPSENE MEVESTPLPI QQNSIQVARS RSTKASVAGE PRLQLRISEI
     VEESLPSVKN NQARRKSNIV KEIEKMKSKR EEQRAQNTEL RIKRAQDYDT SVPNWQFGKM
     IKEFRATMDC HRISMADPAE EHRICVCVRK RPLNKQELSK KEIDIISVPS KNIVLVHEPK
     LKVDLTKYLE NQAFRFDFSF DETATNEVVY RFTARPLVQS IFEGGKATCF AYGQTGSGKT
     HTMGGDFSGK SQNVSKGVYA FASRDVFLLL DQPRYRHLDL EVFVTFFEIY NGKVFDLLNK
     KTKLRVLEDA KQEVQVVGLL EKQVTSADDV FKMIEIGSAC RTSGQTFANT SSSRSHACLQ
     IILRRGRKLH GKFSLVDLAG NERGADTASA DRITRMEGAE INRSLLALKE CIRALGQNKS
     HTPFRESKLT QILRDSFIGE NSRTCMIAML SPGFNSCEYT LNTLRYADRV KELSPQNAET
     NDDNLQMDTE DSDESHASIG GLELQDDKDE ELSTHNSFQD ALHRVGELED KAVDELRELV
     QREPEWTNLL QMTEQPDYDL ENFVMQAEYL IQERSKVLIA LGDSINSLRL ALQVEERASK
     QISKKRRFNK
//
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