KIF19_MOUSE
ID KIF19_MOUSE Reviewed; 997 AA.
AC Q99PT9; A7DTH0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Kinesin-like protein KIF19;
GN Name=Kif19; Synonyms=Kif19a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-255, AND TISSUE SPECIFICITY.
RX PubMed=11416179; DOI=10.1073/pnas.111145398;
RA Miki H., Setou M., Kaneshiro K.;
RT "All kinesin superfamily protein, KIF, genes in mouse and human.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7004-7011(2001).
RN [3]
RP PROTEIN SEQUENCE OF 335-347, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23168168; DOI=10.1016/j.devcel.2012.10.016;
RA Niwa S., Nakajima K., Miki H., Minato Y., Wang D., Hirokawa N.;
RT "KIF19A is a microtubule-depolymerizing kinesin for ciliary length
RT control.";
RL Dev. Cell 23:1167-1175(2012).
CC -!- FUNCTION: Plus end-directed microtubule-dependent motor protein that
CC regulates the length of motile cilia by mediating depolymerization of
CC microtubules at ciliary tips. {ECO:0000269|PubMed:23168168}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:23168168}. Cell projection, cilium
CC {ECO:0000269|PubMed:23168168}. Note=Localizes to cilia tips.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the oviduct and trachea.
CC Expressed in testis, lung, ovary and brain.
CC {ECO:0000269|PubMed:11416179, ECO:0000269|PubMed:23168168}.
CC -!- DISRUPTION PHENOTYPE: Mice show growth retardation, higher mortality (4
CC weeks after birth) and display hydrocephalus as well as female
CC infertility. Female infertility is probably caused by fallopian tube
CC obstruction. Phenotypes are due to abnormally elongated cilia that
CC cannot generate proper fluid flow. {ECO:0000269|PubMed:23168168}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AL663079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB054026; BAB32490.1; -; Genomic_DNA.
DR CCDS; CCDS36367.1; -.
DR RefSeq; NP_001096085.1; NM_001102615.1.
DR PDB; 5GSY; EM; 7.00 A; K=1-353.
DR PDB; 5GSZ; X-ray; 2.72 A; A=1-353.
DR PDBsum; 5GSY; -.
DR PDBsum; 5GSZ; -.
DR AlphaFoldDB; Q99PT9; -.
DR SMR; Q99PT9; -.
DR BioGRID; 235048; 35.
DR IntAct; Q99PT9; 35.
DR STRING; 10090.ENSMUSP00000081398; -.
DR iPTMnet; Q99PT9; -.
DR PhosphoSitePlus; Q99PT9; -.
DR jPOST; Q99PT9; -.
DR PaxDb; Q99PT9; -.
DR PRIDE; Q99PT9; -.
DR ProteomicsDB; 263445; -.
DR Antibodypedia; 31955; 88 antibodies from 20 providers.
DR Ensembl; ENSMUST00000084368; ENSMUSP00000081398; ENSMUSG00000010021.
DR GeneID; 286942; -.
DR KEGG; mmu:286942; -.
DR UCSC; uc007mfq.1; mouse.
DR CTD; 286942; -.
DR MGI; MGI:2447024; Kif19a.
DR VEuPathDB; HostDB:ENSMUSG00000010021; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000160989; -.
DR HOGENOM; CLU_001485_15_0_1; -.
DR InParanoid; Q99PT9; -.
DR OMA; QGRLFMV; -.
DR OrthoDB; 488751at2759; -.
DR PhylomeDB; Q99PT9; -.
DR TreeFam; TF331721; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 286942; 2 hits in 70 CRISPR screens.
DR PRO; PR:Q99PT9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99PT9; protein.
DR Bgee; ENSMUSG00000010021; Expressed in islet of Langerhans and 48 other tissues.
DR ExpressionAtlas; Q99PT9; baseline and differential.
DR GO; GO:0005930; C:axoneme; IEA:GOC.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
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:0008574; F:plus-end-directed microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0060404; P:axonemal microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0070462; P:plus-end specific microtubule depolymerization; IMP:UniProtKB.
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 3D-structure; ATP-binding; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..997
FT /note="Kinesin-like protein KIF19"
FT /id="PRO_0000278246"
FT DOMAIN 11..346
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 477..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 361..388
FT /evidence="ECO:0000255"
FT COILED 506..551
FT /evidence="ECO:0000255"
FT COMPBIAS 477..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 108
FT /note="C -> T (in Ref. 2; BAB32490)"
FT /evidence="ECO:0000305"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:5GSZ"
FT TURN 137..141
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 220..233
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:5GSZ"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:5GSZ"
FT STRAND 315..323
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5GSZ"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:5GSZ"
SQ SEQUENCE 997 AA; 111559 MW; 35A8114D7D2757E3 CRC64;
MKDSGDSKDQ QLMVALRVRP ISVAELEEGA TLIAHKMDEQ MVVLMDPMED PDDILRAHRS
REKSYLFDVA FDFTATQEMV YQATTKSLIE GVISGYNATV FAYGPTGCGK TYTMLGTDHE
PGIYVRTLND LFRAIEETSN DMEYEVSMSY LEIYNEMIRD LLNPALGYLE LREDSKGVIQ
VAGITEVSTI NAKEIMQLLM KGNRQRTQEP TAANQTSSRS HAVLQVAVRQ RSRVKNILQE
VRQGRLFMID LAGSERASQT QNRGQRMKEG AHINRSLLAL GNCINALSDK GSNKYINYRD
SKLTRLLKDS LGGNSRTVMI AHISPASTAF EESRNTLTYA GRAKNIRTRV KQNLLNVSYH
IAQYTSIIAD LRGEIQRLKC KIDQQAGRGQ ARGKLDRGDI RHIQAEVQLH SGQEGPAEMG
QLREQLISAF HEQMDVRRRL LELENQAMEV QIDTSRHLLT IAGWEHEKSR RALKWREERR
KESYTKEDSE KDSDTGDEPD NLEPPEVASA RENIAALVGE QKKLRKEKLA LEQRCRELRA
RGRRLEETLP RRIGSEEQRE VLSLLCRVHE LEVENTEMQS HALLRDSALR HRREAVRRLE
QHRSLCDEII QGQRQIIDDY NLEVPRHLEE LYEVYLRELE EGSLERATIM DRVASRALQD
SSLPKITPAG ATLTPDSDLE SVKTLSSEAQ RPQNNTLPPL GTDSESYHVF KASPRAWQVK
SSSVPTPPPI QVGSLVTQEA PPQDSLGSQI NSSPESSENL SEILLSHKER KEILTRTKCI
SVKAAQRRSR ALGTEGRHLL APATERSSLS LHSLSEADDA RPPGQLACKR PPSPTLQHAI
SEDNLSSSTG EGPSRAVGPR GDGTGSWVRG QKKCLSKKRE ESLEAKRRKR RSRSFEVTGQ
GLSRPKTHLL GPRPSEGLSD RRMPACGRPS PGVRHLGKVS LPLAKVKFPP NQNTGSGNPS
PLLVAPNQAG VSRRATRGPS LPHGSSTFGK DGRLQHN
