ID A0A1S3EY40_DIPOR Unreviewed; 932 AA.
AC A0A1S3EY40;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=Kifc3 {ECO:0000313|RefSeq:XP_012868357.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012868357.1};
RN [1] {ECO:0000313|RefSeq:XP_012868357.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012868357.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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_012868357.1; XM_013012903.1.
DR AlphaFoldDB; A0A1S3EY40; -.
DR GeneID; 105983124; -.
DR CTD; 3801; -.
DR OrthoDB; 453489at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; cd01366; KISc_C_terminal; 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; PTHR47972:SF5; KINESIN-LIKE PROTEIN KIFC3; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT DOMAIN 551..874
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 28..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 173..338
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 385..451
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 506..537
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 113..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 634..641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 932 AA; 103761 MW; 42C6D3A031250820 CRC64;
MVPSRRTWNL GATPSLRGLW RVGRAPEPEL GMARPAPASP AARPFPHTGP GRLRTGRGKD
TPVSGDEDPS TRIAARPALA QCRALSVDWA GPGSPHRLYL TVQQALQDKG CESKSQGTKE
DKLLKRPAPR RDREAPEAGG RMNIEKTGKG GGRLFGSGRC SSLSGSPGAA PVVHRMVEAM
SQLQEEKSQL QEELVVLRER LALHDSDQHA TSTQLQNQVE NLKEKLISQA QEVSRLRSEL
GGTDLEKHRD RLMVENERLR QELQELRAQP AAPCPGCEHS QESTQLRDKL SQLQLEVAEN
KGMLSELNLE VQQKTDRLAE VELRLKDCLA EKAQEEERLS RRLRDSHETI ASLRAQSPPV
KYVIKTVEVE SSKTKQALSE SQARNQHLQE QVAMQRQVLK EMEQQLHSSH QLTAQLRAQI
AMYEAELERA HGQMLEEMQS LEEDKNRAIE EAFARAQVEM KAVHENLAGV RTNLLTLQPA
LRTLTNDYNG LKRQVRGFPM LLQEALRSVK AEIGQAIEEV NNNNQELLRK YRRELQLRKK
CHNELVRLKG NIRVIARVRP VTKEDGEGPE ATNAVTFDPD DDSIIHLLHK GKPVSFELDK
VFSPGASQQD VFQEVQALIT SCIDGFNVCI FAYGQTGAGK TYTMEGTPEN PGINQRALQL
LFSEVQEKAS DWQYTITVSA AEIYNEVLRD LLGREPQEKL EIRLCPDGSG QLYVPGLTEF
QVQSVEDINK VFEFGHTNRT TEFTNLNEHS SRSHALLIVT VRGVDCSTGL RTIGKLNLVD
LAGSERVGKS GAEGHRLREA QHINKSLSAL GDVIAALRSR QGHVPFRNSK LTYLLQDSLS
GDSKTLMVVQ VSPVEKNASE TLYSLKFAER VRSVELGPGS RRTELGSWSS QEHLEWEPAC
QTPQPSARAH SAPTSGTSSR PGSIRRKLQP SA
//