ID   KIF19_XENLA             Reviewed;         997 AA.
AC   Q7ZXX2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Kinesin-like protein KIF19;
GN   Name=kif19;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC       projection, cilium {ECO:0000250}. Note=Localizes to cilia tips.
CC       {ECO:0000250}.
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; BC044083; AAH44083.1; -; mRNA.
DR   RefSeq; NP_001079193.1; NM_001085724.1.
DR   AlphaFoldDB; Q7ZXX2; -.
DR   SMR; Q7ZXX2; -.
DR   PRIDE; Q7ZXX2; -.
DR   DNASU; 373792; -.
DR   GeneID; 373792; -.
DR   KEGG; xla:373792; -.
DR   CTD; 373792; -.
DR   Xenbase; XB-GENE-5954830; kif19.S.
DR   OMA; QGRLFMV; -.
DR   OrthoDB; 488751at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 373792; Expressed in internal ear and 12 other tissues.
DR   GO; GO:0005930; C:axoneme; IEA:GOC.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; ISS:UniProtKB.
DR   GO; GO:0060404; P:axonemal microtubule depolymerization; ISS:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0070462; P:plus-end specific microtubule depolymerization; ISS: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   2: Evidence at transcript level;
KW   ATP-binding; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..997
FT                   /note="Kinesin-like protein KIF19"
FT                   /id="PRO_0000278247"
FT   DOMAIN          11..346
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          468..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          848..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          360..437
FT                   /evidence="ECO:0000255"
FT   COILED          508..577
FT                   /evidence="ECO:0000255"
FT   COILED          861..889
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        468..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..890
FT                   /note="Basic and acidic 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"
SQ   SEQUENCE   997 AA;  114977 MW;  0084DE72604B693D CRC64;
     MKDGGESKEQ QLTVALRIRP INETELAEGA TIIAHKVDKQ MVVLMDPMED SDDILRANRS
     REKSYMFDVA FDYTATQDTV YRFTTKGLIE GVISGYNATV FAYGPTGCGK TYTMLGTDWE
     PGIYIRTLND LFKAIEETSD DMEYEVLMSY MEIYNEMIRD LLNPSLGYLD LREDSKGVIQ
     VAGITEVSTI NAKEIMQLLM KGNRQRTQEP TAANKTSSRS HAILQVTVRQ KSRVKNITQE
     VRVGRLFMID LAGSERASQT QNRGLRMKEG AHINRSLLAL GNCINALSER GSNKYVNYRD
     SKLTRLLKDS LGGNSRTVMI AHISPASTSF EESRNTLTYA DRAKNIKTRV KRNLLNVSYH
     IAQYTSIISD LRKEIQRLKK KIDEQGLKQI RSEKSDIRNI QAEVQLHSST YGRHEMEQLK
     EQLIRAFREQ MDIRRQLMEI ENSSMEMQME TSRHFLITAE WEQEKTRRAR KWRDEHRKET
     YGKDDSEKDS DTGDDQSDFI EPPEVITARE TIQILEGDQN KLRRQKLELE KRFRDVRHHA
     RRLEEALPKR ISSDDQREIL SLLCKVHELE IENTEMQSHA LLKDNMIRQK DYMVQRFEQH
     RSLCDEIIQQ QRRIIYDHNL TVPHQLNDLY ELYFRELEEG VLDKAAVLAL KDSQSCLPKI
     PNLTAEENLQ EPDSDQESVR TFGSDNRNPI HRDSYKNLLP QILSETDSDT NKVFKTSPRA
     RHLKNGAVVT PPPIHVNGII SKEYLPRNQI NYFPDSTDSK VVLTHREKKE ITTSIQSIAV
     KAARRRSRVL EGDRLQPMKE RSNLSVHSMS ESEDTVFTDQ RFPSSSLHHA ASEDNLSSTT
     GEIVAVHGGG SNHRDSPNLW HRTQKKQAQK LEKREESLEV KRRKKRSRSF EVTGQGLVRP
     KNHISRNRAL ESNSDHKIQS NTLQTNRKIM LPIAQVKLPQ NQTTTVFKMA EQQEGKHQTN
     QPGSVKKLIS TNQPPRFNYI NANASGIYVK DVRVRKY