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KIF17_HUMAN
ID   KIF17_HUMAN             Reviewed;        1029 AA.
AC   Q9P2E2; A2A3Q7; A2A3Q8; O95077; Q53YS6; Q5VWA9; Q6GSA8; Q8N411;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Kinesin-like protein KIF17;
DE   AltName: Full=KIF3-related motor protein;
GN   Name=KIF17; Synonyms=KIAA1405, KIF3X;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS MET-402 AND GLU-933.
RX   PubMed=14673085; DOI=10.1073/pnas.2536695100;
RA   Chennathukuzhi V., Morales C.R., El-Alfy M., Hecht N.B.;
RT   "The kinesin KIF17b and RNA-binding protein TB-RBP transport specific cAMP-
RT   responsive element modulator-regulated mRNAs in male germ cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:15566-15571(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS MET-402
RP   AND GLU-933.
RC   TISSUE=Eye;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-1029 (ISOFORM 1), AND VARIANTS
RP   MET-402 AND GLU-933.
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [5]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 793-1029, AND VARIANT GLU-933.
RA   Nagata K., Puls A., Futter C., Aspenstroem P., Hall A.;
RT   "The MAP kinase kinase kinases MLK2 and MLK3 are targets for RAC/Cdc42 and
RT   components of microtubule motor complexes.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dendrite-specific motor protein which, in association with
CC       the Apba1-containing complex (LIN-10-LIN-2-LIN-7 complex), transports
CC       vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B
CC       along microtubules. {ECO:0000250|UniProtKB:Q99PW8}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with APBA1 (via PDZ
CC       domain); the interaction is direct and is required for association of
CC       KIF17 with the cargo that is to be transported (By similarity).
CC       Interacts with IFT B complex components IFT52 and IFT57 (By
CC       similarity). Interacts with TTC30B (By similarity). Interacts with
CC       PIWIL1 (By similarity). Interacts with TBATA (By similarity).
CC       {ECO:0000250|UniProtKB:Q99PW8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC       projection, cilium {ECO:0000250|UniProtKB:Q99PW8}. Cell projection,
CC       dendrite {ECO:0000250|UniProtKB:Q99PW8}. Note=Localizes to dendrites of
CC       pyramidal neurons (By similarity). Does not localize to the axons or
CC       nuclei in cerebral cortex, hippocampus or olfactory bulb (By
CC       similarity). Co-localizes with NR2B-containing vesicles along
CC       microtubules (By similarity). {ECO:0000250|UniProtKB:Q99PW8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=KIF17b;
CC         IsoId=Q9P2E2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P2E2-3; Sequence=VSP_040346;
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD01428.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAD01428.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC       Sequence=AAH36871.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
CC       Sequence=BAA92643.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR   EMBL; AY484427; AAR33039.1; -; mRNA.
DR   EMBL; AL391357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL663074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC036871; AAH36871.1; ALT_SEQ; mRNA.
DR   EMBL; BC065927; AAH65927.1; -; mRNA.
DR   EMBL; AB037826; BAA92643.2; ALT_SEQ; mRNA.
DR   EMBL; AF009624; AAD01428.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS213.1; -. [Q9P2E2-1]
DR   CCDS; CCDS44079.1; -. [Q9P2E2-3]
DR   RefSeq; NP_001116291.1; NM_001122819.2. [Q9P2E2-3]
DR   RefSeq; NP_001274141.1; NM_001287212.1.
DR   RefSeq; NP_065867.2; NM_020816.3. [Q9P2E2-1]
DR   AlphaFoldDB; Q9P2E2; -.
DR   SMR; Q9P2E2; -.
DR   BioGRID; 121629; 7.
DR   IntAct; Q9P2E2; 8.
DR   MINT; Q9P2E2; -.
DR   STRING; 9606.ENSP00000247986; -.
DR   iPTMnet; Q9P2E2; -.
DR   PhosphoSitePlus; Q9P2E2; -.
DR   BioMuta; KIF17; -.
DR   DMDM; 317373436; -.
DR   EPD; Q9P2E2; -.
DR   jPOST; Q9P2E2; -.
DR   MassIVE; Q9P2E2; -.
DR   MaxQB; Q9P2E2; -.
DR   PaxDb; Q9P2E2; -.
DR   PeptideAtlas; Q9P2E2; -.
DR   PRIDE; Q9P2E2; -.
DR   ProteomicsDB; 83790; -. [Q9P2E2-1]
DR   ProteomicsDB; 83791; -. [Q9P2E2-3]
DR   Antibodypedia; 15106; 130 antibodies from 21 providers.
DR   DNASU; 57576; -.
DR   Ensembl; ENST00000247986.2; ENSP00000247986.2; ENSG00000117245.13. [Q9P2E2-1]
DR   Ensembl; ENST00000400463.8; ENSP00000383311.3; ENSG00000117245.13. [Q9P2E2-3]
DR   GeneID; 57576; -.
DR   KEGG; hsa:57576; -.
DR   MANE-Select; ENST00000400463.8; ENSP00000383311.3; NM_001122819.3; NP_001116291.1. [Q9P2E2-3]
DR   UCSC; uc001bdr.6; human. [Q9P2E2-1]
DR   CTD; 57576; -.
DR   DisGeNET; 57576; -.
DR   GeneCards; KIF17; -.
DR   HGNC; HGNC:19167; KIF17.
DR   HPA; ENSG00000117245; Tissue enriched (testis).
DR   MIM; 605037; gene.
DR   neXtProt; NX_Q9P2E2; -.
DR   OpenTargets; ENSG00000117245; -.
DR   PharmGKB; PA38809; -.
DR   VEuPathDB; HostDB:ENSG00000117245; -.
DR   eggNOG; KOG0239; Eukaryota.
DR   GeneTree; ENSGT00940000158776; -.
DR   HOGENOM; CLU_001485_22_0_1; -.
DR   InParanoid; Q9P2E2; -.
DR   OMA; KKEAVWD; -.
DR   OrthoDB; 862274at2759; -.
DR   PhylomeDB; Q9P2E2; -.
DR   TreeFam; TF105223; -.
DR   PathwayCommons; Q9P2E2; -.
DR   Reactome; R-HSA-5620924; Intraflagellar transport.
DR   Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR   SignaLink; Q9P2E2; -.
DR   BioGRID-ORCS; 57576; 14 hits in 1073 CRISPR screens.
DR   GeneWiki; KIF17; -.
DR   GenomeRNAi; 57576; -.
DR   Pharos; Q9P2E2; Tbio.
DR   PRO; PR:Q9P2E2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9P2E2; protein.
DR   Bgee; ENSG00000117245; Expressed in left testis and 101 other tissues.
DR   ExpressionAtlas; Q9P2E2; baseline and differential.
DR   Genevisible; Q9P2E2; HS.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0032839; C:dendrite 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:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:1990075; C:periciliary membrane compartment; IEA:Ensembl.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
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:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR   GO; GO:0030030; P:cell projection organization; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1029
FT                   /note="Kinesin-like protein KIF17"
FT                   /id="PRO_0000125450"
FT   DOMAIN          5..335
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          523..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          968..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          346..462
FT                   /evidence="ECO:0000255"
FT   COILED          739..846
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        532..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..673
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..992
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1029
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         91..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   VAR_SEQ         908
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040346"
FT   VARIANT         341
FT                   /note="I -> V (in dbSNP:rs2296225)"
FT                   /id="VAR_055983"
FT   VARIANT         369
FT                   /note="S -> R (in dbSNP:rs56750936)"
FT                   /id="VAR_061282"
FT   VARIANT         402
FT                   /note="V -> M (in dbSNP:rs522496)"
FT                   /evidence="ECO:0000269|PubMed:10718198,
FT                   ECO:0000269|PubMed:14673085, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_023527"
FT   VARIANT         675
FT                   /note="V -> I (in dbSNP:rs558760)"
FT                   /id="VAR_055984"
FT   VARIANT         735
FT                   /note="V -> I (in dbSNP:rs13375609)"
FT                   /id="VAR_055985"
FT   VARIANT         933
FT                   /note="D -> E (in dbSNP:rs631357)"
FT                   /evidence="ECO:0000269|PubMed:10718198,
FT                   ECO:0000269|PubMed:14673085, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.6"
FT                   /id="VAR_023528"
FT   CONFLICT        925
FT                   /note="D -> Y (in Ref. 6; AAD01428)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        957
FT                   /note="R -> W (in Ref. 1; AAR33039 and 4; BAA92643)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1029 AA;  115068 MW;  ED1B7F9806CC9AF6 CRC64;
     MASEAVKVVV RCRPMNQRER ELRCQPVVTV DCARAQCCIQ NPGAADEPPK QFTFDGAYHV
     DHVTEQIYNE IAYPLVEGVT EGYNGTIFAY GQTGSGKSFT MQGLPDPPSQ RGIIPRAFEH
     VFESVQCAEN TKFLVRASYL EIYNEDVRDL LGADTKQKLE LKEHPEKGVY VKGLSMHTVH
     SVAQCEHIME TGWKNRSVGY TLMNKDSSRS HSIFTISIEM SAVDERGKDH LRAGKLNLVD
     LAGSERQSKT GATGERLKEA TKINLSLSAL GNVISALVDG RCKHVPYRDS KLTRLLQDSL
     GGNTKTLMVA CLSPADNNYD ETLSTLRYAN RAKNIRNKPR INEDPKDALL REYQEEIKKL
     KAILTQQMSP SSLSALLSRQ VPPDPVQVEE KLLPQPVIQH DVEAEKQLIR EEYEERLARL
     KADYKAEQES RARLEEDITA MRNSYDVRLS TLEENLRKET EAVLQVGVLY KAEVMSRAEF
     ASSAEYPPAF QYETVVKPKV FSTTDTLPSD DVSKTQVSSR FAELPKVEPS KSEISLGSSE
     SSSLEETSVS EAFPGPEEPS NVEVSMPTEE SRSRYFLDEC LGQEAAGHLL GEQNYLPQEE
     PQEVPLQGLL GLQDPFAEVE AKLARLSSTV ARTDAPQADV PKVPVQVPAP TDLLEPSDAR
     PEAEAADDFP PRPEVDLASE VALEVVRTAE PGVWLEAQAP VALVAQPEPL PATAGVKRES
     VGMEVAVLTD DPLPVVDQQQ VLARLQLLEQ QVVGGEQAKN KDLKEKHKRR KRYADERRKQ
     LVAALQNSDE DSGDWVLLNV YDSIQEEVRA KSKLLEKMQR KLRAAEVEIK DLQSEFQLEK
     IDYLATIRRQ ERDSMLLQQL LEQVQPLIRR DCNYSNLEKI LRESCWDEDN GFWKIPHPVI
     TKTSLPVAVS TGPQNKPARK TSAADNGEPN MEDDRYRLML SRSNSENIAS NYFRSKRASQ
     ILSTDARKSL THHNSPPGLS CPLSNNSAIP PTQAPEMPQP RPFRLESLDI PFTKAKRKKS
     KSNFGSEPL
 
 
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