KIFC1_RAT
ID KIFC1_RAT Reviewed; 693 AA.
AC Q5XI63; O54719;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Kinesin-like protein KIFC1;
DE AltName: Full=Kinesin-related protein 1;
GN Name=Kifc1 {ECO:0000312|EMBL:AAH83827.1, ECO:0000312|RGD:1359118};
GN Synonyms=Krp1 {ECO:0000312|EMBL:AAB88699.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH83827.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH83827.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB88699.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 426-588.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAB88699.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAB88699.1};
RX PubMed=8688559; DOI=10.1091/mbc.7.2.289;
RA Sperry A.O., Zhao L.-P.;
RT "Kinesin-related proteins in the mammalian testes: candidate motors for
RT meiosis and morphogenesis.";
RL Mol. Biol. Cell 7:289-305(1996).
CC -!- FUNCTION: Minus end-directed microtubule-dependent motor required for
CC bipolar spindle formation. May contribute to movement of early
CC endocytic vesicles. Regulates cilium formation and structure.
CC {ECO:0000250|UniProtKB:Q9QWT9}.
CC -!- SUBUNIT: Binds NUBP1 and NUBP2. Interacts with PPP1R42 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QWT9}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9QWT9}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9QWT9}. Early endosome
CC {ECO:0000250|UniProtKB:Q9QWT9}. Note=Associated with nucleus during
CC interphase, centrosomes in early and spindle in later mitosis.
CC {ECO:0000250|UniProtKB:Q9QWT9}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; BC083827; AAH83827.1; -; mRNA.
DR EMBL; AF035951; AAB88699.1; -; mRNA.
DR RefSeq; NP_001005878.1; NM_001005878.1.
DR AlphaFoldDB; Q5XI63; -.
DR SMR; Q5XI63; -.
DR STRING; 10116.ENSRNOP00000061875; -.
DR PaxDb; Q5XI63; -.
DR PRIDE; Q5XI63; -.
DR GeneID; 294286; -.
DR KEGG; rno:294286; -.
DR UCSC; RGD:1359118; rat.
DR CTD; 3833; -.
DR RGD; 1359118; Kifc1.
DR VEuPathDB; HostDB:ENSRNOG00000000479; -.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_4_1; -.
DR InParanoid; Q5XI63; -.
DR OMA; TWTYHDE; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; Q5XI63; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:Q5XI63; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000479; Expressed in thymus and 18 other tissues.
DR Genevisible; Q5XI63; RN.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR Gene3D; 3.40.850.10; -; 1.
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 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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endosome; Microtubule; Mitosis; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..693
FT /note="Kinesin-like protein KIFC1"
FT /id="PRO_0000302090"
FT DOMAIN 330..683
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..334
FT /evidence="ECO:0000255"
FT COMPBIAS 63..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 430..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW19"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW19"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW19"
SQ SEQUENCE 693 AA; 76141 MW; 739A2EC8DD1845FE CRC64;
MRGRGSRDTG TQSAAFASRP VRTTVDMQAQ RAPLMEVKRN LELSTTLVKS SSRLPLPGSR
LKRGPDQMED GLEPAKKRTR GMGTVTKVDT SRPRGPPLSA VSTAAQKGPR KTGPRGCSAV
GPVLRNQKPA PAAPAQKPGT STAPAVAGKK PGKRPAWDLK GQLCDLHEEL KQYREKTQTL
DRENQGLREQ LREVQEQATT LGTERNTLEE ELASVRRRAE QSQQKLETLG ARVLELEECL
GTKERLVQEL QTERLQLQEE RSTLSTQLEE REREFQASEA ALSSSRAEVL CLRQKTAAQV
TLLAEQGDRL YGLEMERRRL HNQLQELKGN IRVFCRVRPV LEGESTPSPG FLVFPPGPAG
PSDPPTRLCL SRSDDRRSTL TRAPAAATRH DFSFDRVFPP GSKQEEVFEE ISMLVQSALD
GYPVCIFAYG QTGSGKTFTM EGGPRGDPQL EGLIPRAMRH LFSVAQEMSG QGWTYSFVAS
YVEIYNETVR DLLATGTRKG QGGDCEIRRA GPGSEELTVT NARYVPVSCE KEVEALLHLA
QQNRAVARTA QNERSSRSHS VFQLQISGEH AARGLQCGAP LNLVDLAGSE RLDPGLTLGP
GERDRLRETQ AINSSLSTLG LVIMALSNKE SHVPYRNSKL TYLLQNSLGG SAKMLMFVNI
SPLEENVSES LNSLRFASKV NQCVIGTAQA NKK
