KIF1A_RAT
ID KIF1A_RAT Reviewed; 1707 AA.
AC F1M4A4;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Kinesin-like protein KIF1A;
GN Name=Kif1a {ECO:0000312|RGD:1304996};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION, INTERACTION WITH SYT4, AND SUBCELLULAR LOCATION.
RX PubMed=29166604; DOI=10.1016/j.celrep.2017.10.084;
RA Bharat V., Siebrecht M., Burk K., Ahmed S., Reissner C.,
RA Kohansal-Nodehi M., Steubler V., Zweckstetter M., Ting J.T., Dean C.;
RT "Capture of Dense Core Vesicles at Synapses by JNK-Dependent
RT Phosphorylation of Synaptotagmin-4.";
RL Cell Rep. 21:2118-2133(2017).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CALM1; PPFIA2; SYT4; SYT11
RP AND TANC2, AND MUTAGENESIS OF 723-TRP--LEU-731.
RX PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071;
RA Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I.,
RA Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.;
RT "Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls
RT DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.";
RL Cell Rep. 24:685-700(2018).
CC -!- FUNCTION: Motor for anterograde axonal transport of synaptic vesicle
CC precursors (Probable). Also required for neuronal dense core vesicles
CC (DCVs) transport to the dendritic spines and axons (PubMed:29166604,
CC PubMed:30021165). The interaction calcium-dependent with CALM1
CC increases vesicle motility and interaction with the scaffolding
CC proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites
CC (PubMed:30021165). {ECO:0000269|PubMed:29166604,
CC ECO:0000269|PubMed:30021165, ECO:0000305}.
CC -!- SUBUNIT: Monomer. Interacts with PPFIA1 and PPFIA4 (By similarity).
CC Interacts with CALM1; the interaction is increased in presence of
CC calcium and increases neuronal dense core vesicles motility
CC (PubMed:30021165). Interacts with PPFIA2 and TANC2; both interactions
CC allow the recruitment of neuronal dense core vesicles to dendritic
CC spines and decrease in presence of calcium (PubMed:30021165). Interacts
CC with SYT4 (unphosphorylated) and SYT11; both interactions increase in
CC presence of calcium (PubMed:30021165, PubMed:29166604). Interacts with
CC MADD (By similarity). {ECO:0000250|UniProtKB:P33173,
CC ECO:0000269|PubMed:29166604, ECO:0000269|PubMed:30021165}.
CC -!- INTERACTION:
CC F1M4A4; A0A142I9X8: US9; Xeno; NbExp=5; IntAct=EBI-11691394, EBI-11890817;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q12756}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q12756}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P33173}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P33173}. Synapse {ECO:0000250|UniProtKB:P33173}.
CC Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle
CC membrane {ECO:0000269|PubMed:29166604, ECO:0000269|PubMed:30021165};
CC Peripheral membrane protein {ECO:0000305|PubMed:30021165}; Cytoplasmic
CC side {ECO:0000305|PubMed:30021165}. Note=Within neuronal cells
CC concentrated in the axon, with smaller amounts in the perinuclear and
CC synaptic regions (By similarity). Expressed in distal regions of
CC neurites. {ECO:0000250|UniProtKB:P33173, ECO:0000250|UniProtKB:Q12756}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AABR07068350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017452401.1; XM_017596912.1.
DR RefSeq; XP_017459418.1; XM_017603929.1.
DR AlphaFoldDB; F1M4A4; -.
DR SMR; F1M4A4; -.
DR IntAct; F1M4A4; 1.
DR STRING; 10116.ENSRNOP00000038927; -.
DR jPOST; F1M4A4; -.
DR PaxDb; F1M4A4; -.
DR PRIDE; F1M4A4; -.
DR GeneID; 363288; -.
DR KEGG; rno:363288; -.
DR CTD; 547; -.
DR RGD; 1304996; Kif1a.
DR VEuPathDB; HostDB:ENSRNOG00000023993; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_10_1_1; -.
DR InParanoid; F1M4A4; -.
DR OMA; KITICHE; -.
DR OrthoDB; 76316at2759; -.
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:F1M4A4; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000023993; Expressed in frontal cortex and 13 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098674; C:extrinsic component of neuronal dense core vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098992; C:neuronal dense core vesicle; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:RGD.
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:0008089; P:anterograde axonal transport; IMP:RGD.
DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; IGI:ARUK-UCL.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0099519; P:dense core granule cytoskeletal transport; IMP:UniProtKB.
DR GO; GO:0022027; P:interkinetic nuclear migration; IMP:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0098840; P:protein transport along microtubule; IDA:RGD.
DR GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; IGI:ARUK-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 2.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Membrane; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..1707
FT /note="Kinesin-like protein KIF1A"
FT /id="PRO_0000448662"
FT DOMAIN 5..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 525..581
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 1592..1690
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 657..1105
FT /note="Required for interaction with CALM1, PPFIA2 and
FT TANC2"
FT /evidence="ECO:0000269|PubMed:30021165"
FT REGION 1424..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 637..671
FT /evidence="ECO:0000255"
FT COMPBIAS 1426..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 723..731
FT /note="WKWYQFTSL->AKAAQATSA: Abolishes interaction with
FT CALM1. Decreases interaction with SYT4 and SYT11. Abolishes
FT location to neuronal dense core vesicles."
FT /evidence="ECO:0000269|PubMed:30021165"
SQ SEQUENCE 1707 AA; 192934 MW; 7875216D504B2427 CRC64;
MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKETPKSF SFDYSYWSHT
SPEDINYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEKDQQGIIP
QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETNITTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAII
NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD ITDTNTVPGG PKLTNALVGM SPSSSLSALS
SRAASVSSLH ERILFAPGSE EAIERLKETE KIIAELNETW EEKLRRTEAI RMEREALLAE
MGVAMREDGG TLGVFSPKKT PHLVNLNEDP LMSECLLYYI KDGVTRVGRE DAERRQDIVL
SGHFIKEEHC IFRSDSRGGG EAVVTLEPCE GADTYVNGKK VTEPSILRSG NRIIMGKSHV
FRFNHPEQAR QERERTPCAE TPAEPVDWAF AQRELLEKQG IDMKQEMEQR LQELEDQYRR
EREEATYLLE QQRLDYESKL EALQKQMDSR YYPEVNEEEE EPEDEVQWTE RECELALWAF
RKWKWYQFTS LRDLLWGNAI FLKEANAISV ELKKKVQFQF VLLTDTLYSP LPPDLLPPEA
AKDRETRPFP RTIVAVEVQD QKNGATHYWT LEKLRQRLDL MREMYDRAAE VPSSVVEDCD
NVVTGGDPFY DRFPWFRLVG RAFVYLSNLL YPVPLVHRVA IVSEKGEVKG FLRVAVQAIS
ADEEAPDYGS GVRQSGTAKI SFDDQHFEKF QSESCPVVGM SRSGTSQEEL RIVEGQGQGA
DAGPSADEVN NNTCSAVPPE GLLDSPEKAA LDGPLDTALD HLRLGSTFTF RVTVLQASSI
SAEYADIFCQ FNFIHRHDEA FSTEPLKNTG RGPPLGFYHV QNIAVEVTKS FIEYIKSQPI
VFEVFGHYQQ HPFPPLCKDV LSPLRPSRRH FPRVMPLSKP VPATKLSTMT RPSPGPCHCK
YDLLVYFEIC ELEANGDYIP AVVDHRGGMP CMGTFLLHQG IQRRITVTLL HETGSHIRWK
EVRELVVGRI RNTPETDEAL IDPNILSLNI LSSGYVHPAQ DDRQFLDSDI PRTFYQFEAA
WDSSMHNSLL LNRVTPYREK IYMTLSAYIE MENCTQPAVI TKDFCMVFYS RDAKLPASRS
IRNLFGSGSL RATEGNRVTG VYELSLCHVA DAGSPGMQRR RRRVLDTSVA YVRGEENLAG
WRPRSDSLIL DHQWELEKLS LLQEVEKTRH YLLLREKLET TQRPVPEVLS PASSEDSESR
SSSGASSPLS AEGQPSPLEV PNERQRELAV KCLRLLMHTF NREYTHSHVC ISASESKLSE
MSVTLMRDPS MSPLGAATLT PSSTCPSLIE GRYGATDVRT PQPCSRPASP EPELLPELDS
KKTPSPVRAT ETEKEPQRLL VPDIQEIRVS PIVSKKGYLH FLEPHTAGWA KRFVVVRRPY
AYMYNSDKDT VERFVLNLST AQVEYSEDQQ AMLKTPNTFA VCTEHRGILL QANSDKDMHD
WLYAFNPLLA GTIRSKLSRR RSAQMRV
