ID   KRP85_STRPU             Reviewed;         699 AA.
AC   P46872;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Kinesin-II 85 kDa subunit;
DE   AltName: Full=KRP-85/95 85 kDa subunit;
GN   Name=KRP85;
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}.
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DR   EMBL; L16993; AAA16098.1; -; mRNA.
DR   PIR; S38982; S38982.
DR   RefSeq; NP_999777.1; NM_214612.1.
DR   AlphaFoldDB; P46872; -.
DR   SMR; P46872; -.
DR   STRING; 7668.SPU_018378-tr; -.
DR   EnsemblMetazoa; NM_214612; NP_999777; GeneID_373466.
DR   GeneID; 373466; -.
DR   KEGG; spu:373466; -.
DR   CTD; 373466; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   InParanoid; P46872; -.
DR   OMA; QHMALAH; -.
DR   OrthoDB; 862274at2759; -.
DR   PhylomeDB; P46872; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
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:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR   GO; GO:0060271; P:cilium assembly; 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..699
FT                   /note="Kinesin-II 85 kDa subunit"
FT                   /id="PRO_0000125401"
FT   DOMAIN          10..342
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          369..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..699
FT                   /note="Globular"
FT                   /evidence="ECO:0000250"
FT   REGION          660..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          341..619
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        376..392
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   699 AA;  78697 MW;  7B3866111CB08190 CRC64;
     MPGGSSGNDN VRVVVRCRPL NSKETGQGFK SVVKMDEMRG TVQVTNPNAP SGEPPKSFTF
     DTVFAPGAKQ TDVYNQTARP IVDAIIEGYN GTIFAYGQTG TGKTFTMEGV RSQPELRGII
     PNSFAHIFGH IAKEQENVRF LVRVSYLEIY NEEVKDLLGK DQQHRLEVKE RPDVGVYVKD
     LSAFVVNNAD DMDRIMTLGN KNRSVGATNM NESSSRSHAI FTITLERSDM GLDKEQHVRV
     GKLHMVDLAG SERQTKTGAT GQRLKEATKI NLSLSTLGNV ISSLVDGKST HIPYRNSKLT
     RLLQDSLGGN AKTVMCANIG PAEYNYDETI STLRYANRAK NIKNKAKINE DPKDALLREF
     QKEIEELKKQ ISESGEGLDD DEESGSEESG DEEAGEGGVK KKRKGKNPKR KLSPEIMAAM
     QKKIDEEKKA LEEKKDMVEE DRNTVHRELQ RRESELHKAQ DDQKILNEKL NAIQKKLIVG
     GVDLLAKSEE QEQLLEQSAL EMKERMAKQE SMRKMMEERE QERMDIEEKY SSLQDEAHGK
     TKKLKKVWTM LMQAKSEVAD MQAEHQREME ALLENVRELS RELRLSMLII DSFIPQEFQE
     MIEQYVHWNE DIGEWQLKCV AYTGNNMRKQ TPVADKDKSL AYGEADLSNV FLTYNLEGGG
     MKYKPSQGKS GRPKTSSGRP KTGKKKQASM ASSIDALLQ