ID   KIF7_DANRE              Reviewed;        1363 AA.
AC   Q58G59;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Kinesin-like protein kif7;
DE   AltName: Full=Kinesin-like protein costal2;
GN   Name=kif7; Synonyms=cos2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH GLI1.
RX   PubMed=15647323; DOI=10.1242/dev.01606;
RA   Tay S.Y., Ingham P.W., Roy S.;
RT   "A homologue of the Drosophila kinesin-like protein Costal2 regulates
RT   Hedgehog signal transduction in the vertebrate embryo.";
RL   Development 132:625-634(2005).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH GLI1 AND SUFU.
RX   PubMed=24339784; DOI=10.1371/journal.pgen.1003955;
RA   Maurya A.K., Ben J., Zhao Z., Lee R.T., Niah W., Ng A.S., Iyu A., Yu W.,
RA   Elworthy S., van Eeden F.J., Ingham P.W.;
RT   "Positive and negative regulation of Gli activity by Kif7 in the zebrafish
RT   embryo.";
RL   PLoS Genet. 9:E1003955-E1003955(2013).
CC   -!- FUNCTION: Acts downstream of smo as an intracellular repressor of
CC       hedgehog signaling pathway, mainly through the suppression of gli1
CC       activity. This negative regulatory effect is enhanced in conjunction
CC       with the suppressor of fused (sufu) protein. Positively regulates gli2a
CC       activity by promoting its dissociation from sufu. Involved in the
CC       regulation of microtubular dynamics. {ECO:0000269|PubMed:15647323,
CC       ECO:0000269|PubMed:24339784}.
CC   -!- SUBUNIT: Binds microtubules. Interacts with gli1 and sufu.
CC       {ECO:0000269|PubMed:15647323, ECO:0000269|PubMed:24339784}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:15647323}. Cell projection, cilium {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIF27 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; AY954727; AAX55642.1; -; mRNA.
DR   RefSeq; NP_001014816.1; NM_001014816.1.
DR   AlphaFoldDB; Q58G59; -.
DR   SMR; Q58G59; -.
DR   BioGRID; 95186; 1.
DR   STRING; 7955.ENSDARP00000041576; -.
DR   PaxDb; Q58G59; -.
DR   PRIDE; Q58G59; -.
DR   GeneID; 544651; -.
DR   KEGG; dre:544651; -.
DR   CTD; 374654; -.
DR   ZFIN; ZDB-GENE-050307-1; kif7.
DR   eggNOG; KOG0244; Eukaryota.
DR   InParanoid; Q58G59; -.
DR   PhylomeDB; Q58G59; -.
DR   Reactome; R-DRE-5632684; Hedgehog 'on' state.
DR   SignaLink; Q58G59; -.
DR   PRO; PR:Q58G59; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005929; C:cilium; IDA:ZFIN.
DR   GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR   GO; GO:0035301; C:Hedgehog signaling complex; IDA:ZFIN.
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:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:ZFIN.
DR   GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:ZFIN.
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; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Motor protein; Nucleotide-binding; Reference proteome;
KW   Repressor.
FT   CHAIN           1..1363
FT                   /note="Kinesin-like protein kif7"
FT                   /id="PRO_0000307147"
FT   DOMAIN          15..347
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          603..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1314..1346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          358..385
FT                   /evidence="ECO:0000255"
FT   COILED          491..552
FT                   /evidence="ECO:0000255"
FT   COILED          714..1068
FT                   /evidence="ECO:0000255"
FT   COILED          1116..1225
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        603..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1314..1332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         94..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1363 AA;  154837 MW;  48D8FC5B97F43AB9 CRC64;
     MSPKGVGHSK VEESAVQVAV RVRPLLPKEI LHSHESCITS DPEERRVTLG NDRHFHCDFV
     FEDGSTQEEV YTNCVQPLIE AFFHGFNATV SAYGQTGSGK TYTIGEASIS AFRDDEQGII
     PRAVAEIFKL LDENDLIDFS VRVSYMEVYK EVFRDLLEVE TASKDIHIRE DERGNVVLCG
     VKECEVEGLD EVLSLLESGK TARHTGATQM NPHSSRSHTI FTVLMEQRRG GSRAANGSVQ
     ILSSKFHFVD LAGSERILKT GNTGERLKES IQINSGLLVL GNVIGALGDP KRKGTHIPYR
     DSKITRILKD SLGGNAKTLM IACISPSSSD FDESLNTLNY AKRARNIQNR ATVNCRGEPD
     RIEGLELQIK ALRRALENRQ RSETRIIARS DPEKRLRPFE VDVRKLQAES AHYRTCTDSA
     YRLLTELQGE GTLNAGQILR VKEWLCGVEE ERSGLTSASG LDSGIESSST EDSTALKRRQ
     AVLNNQDLVK EDWRGEREDY TSQLQAQIQQ LEQENTDFLV ALEDAMEQYK QQSDKLQEQQ
     DLIAELHSLL AQPGGAGFLH LKQRPHTAPI NSLLQTPDRL TPPCDSDVGR SLARQLDVGA
     SVDSSSYSEQ TQWDGTHGNT HCESSRKLNR DEDGHMQTTR DKRKSINVTW TKKDIAIPQG
     PFGGTRTALP QTLGLCHPLG MQFNRRTSNS SIGESSVWES VRGFGGEFCS DRGLLQAQQK
     IRELSITIRM KEELIKELVK TGKDAQAMNR QYSRKISELE AEAEQARVEL TEAQKQLQEL
     EVQGGRDAVD RSKAQECRRK IAAAQSKVQV LKQKQRDTAQ LASLSAQSER RVQELERNVQ
     NMKQQQDLLQ RRLREESQQK RRLETEMQKG KHRVKELEIK NEQQQKILRI KTEEIAAFQR
     QRRSGSNGSV VSLEEQQKIE EQKRWLDEEM EKVLDQRRGL EDLEGELTKR EEILAKKEAL
     LWERSGLESK KLRSSQALSQ DLLTLSSRIE SLERELTERN GLLRSGSAQD SQQIRQEISN
     LRQEKELLLK QRVELDDKLR QGNLLSPEEE RTLFQLDEAI EALDAAIEYK NEAITQRQRQ
     LRASGSMLTQ WEMNLMAKLT YLSASETRAL LCKYFDKVVS LREEERRLQM ALAELELRVE
     EQQNLVGWLE AALERQQLEA DRRLTQQQKE HERNIQLLLQ QCREQMDEGL AGRLRQYEGL
     IHNLSKELNF CKIANQELNI KLREMCGPVN LTGEQCKGLN CDSLLLAGAQ SRVAEDVKPI
     IDAERVQKSR EEMREPVNAP LPATWRRSSL PTEDQYTMEE LRQRAACELP NNRIVQPGMN
     STHWSGSTSL PVTRPRREPR RSSLNTAPLY SSSAIIDVRR NPV