ID   KRP95_STRPU             Reviewed;         742 AA.
AC   P46871;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Kinesin-II 95 kDa subunit;
DE   AltName: Full=KRP-85/95 95 kDa subunit;
GN   Name=KRP95;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Egg;
RX   PubMed=8232586; DOI=10.1038/366268a0;
RA   Cole D.G., Chinn S.W., Wedaman K.P., Hall K., Vuong T., Scholey J.M.;
RT   "Novel heterotrimeric kinesin-related protein purified from sea urchin
RT   eggs.";
RL   Nature 366:268-270(1993).
CC   -!- SUBUNIT: Heterotrimer of a 115 kDa subunit (KAP115) and two kinesin-
CC       like subunits of 95 kDa (KRP95) and 85 kDa (KRP85).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Kinesin II subfamily.
CC       {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; U00996; AAA87393.1; -; mRNA.
DR   PIR; S38983; S38983.
DR   RefSeq; NP_999817.1; NM_214652.1.
DR   AlphaFoldDB; P46871; -.
DR   SMR; P46871; -.
DR   STRING; 7668.SPU_026280-tr; -.
DR   EnsemblMetazoa; XM_030992662; XP_030848522; LOC587208.
DR   GeneID; 373530; -.
DR   CTD; 373530; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   HOGENOM; CLU_1615051_0_0_1; -.
DR   InParanoid; P46871; -.
DR   OMA; LESKMLC; -.
DR   OrthoDB; 862274at2759; -.
DR   PhylomeDB; P46871; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
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-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; 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   PANTHER; PTHR24115; PTHR24115; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Microtubule; Motor protein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..742
FT                   /note="Kinesin-II 95 kDa subunit"
FT                   /id="PRO_0000125400"
FT   DOMAIN          8..339
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          365..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..742
FT                   /note="Globular"
FT                   /evidence="ECO:0000250"
FT   REGION          709..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          338..613
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        365..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..409
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         95..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   742 AA;  84202 MW;  47C40A367BAA77B5 CRC64;
     MSKKSAETVK VVVRCRPMNS KEISQGHKRI VEMDNKRGLV EVTNPKGPPG EPNKSFTFDT
     VYDWNSKQID LYDETFRSLV ESVLQGFNGT IFAYGQTGTG KTFTMEGVRS NPELRGVIPN
     SFEHIFTHIA RTQNQQFLVR ASYLEIYQEE IRDLLAKDQK KRLDLKERPD TGVYVKDLSS
     FVTKSVKEIE HVMTVGNNNR SVGSTNMNEH SSRSHAIFII TIECSELGVD GENHIRVGKL
     NLVDLAGSER QAKTGATGDR LKEATKINLS LSALGNVISA LVDGKSSHIP YRDSKLTRLL
     QDSLGGNAKT VMVANMGPAS YNFDETITTL RYANRAKNIK NKPKINEDPK DALLREFQEE
     ISRLKQALDK KGPSDGRKKG KKRKPGEQGG DDDIEDETEE EGDEMDEEEM YKESQQKLEE
     EKEKIMANQS MIAEEKQKLL SEVQKRQGEI KKEHQQKEML EGKIKAMESK LLVGGKSIVD
     HTNEQQRKIE EQRLLLAEEK NRERDMERKL KEQDDKTVEI EGTFSSLQQE VEVKTKKLKK
     LFAKLQSYKS DIQDLQDEHA RERQELEQTQ NELIRELKLK KVIADNFIPV EERTKITTRA
     VFDEETEEWL LTPLAKAEGP SQMAKRPVSA VGNRRPIADY ARMAAQMGGN PRYKAENILS
     VDLDMPNRTT RDYEGPSVAP RVQAALDAAL QDEDDLDLEV QPEVFKAKTK LKKDKVRSKH
     KAVAKPGSNS QLYPQARGLI QK