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Protein

Kinesin-like protein KIF1A

Gene

Kif1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Motor for anterograde axonal transport of synaptic vesicle precursors.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi97 – 1048ATP

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • microtubule binding Source: MGI
  • microtubule motor activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF1A
Alternative name(s):
Axonal transporter of synaptic vesicles
Gene namesi
Name:Kif1a
Synonyms:Atsv, Kif1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:108391. Kif1a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: UniProtKB-KW
  • neuronal cell body Source: MGI
  • neuron projection Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16951695Kinesin-like protein KIF1APRO_0000125406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei416 – 4161PhosphoserineBy similarity
Modified residuei418 – 4181PhosphoserineBy similarity
Modified residuei419 – 4191PhosphoserineBy similarity
Modified residuei607 – 6071PhosphothreonineCombined sources
Modified residuei612 – 6121PhosphothreonineCombined sources
Modified residuei932 – 9321PhosphoserineCombined sources
Modified residuei937 – 9371PhosphoserineBy similarity
Modified residuei1315 – 13151PhosphoserineBy similarity
Modified residuei1342 – 13421PhosphoserineCombined sources
Modified residuei1524 – 15241PhosphothreonineCombined sources
Modified residuei1528 – 15281PhosphothreonineCombined sources
Modified residuei1533 – 15331PhosphoserineCombined sources
Modified residuei1537 – 15371PhosphoserineCombined sources
Modified residuei1553 – 15531PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP33173.
MaxQBiP33173.
PaxDbiP33173.
PRIDEiP33173.

PTM databases

iPTMnetiP33173.
PhosphoSiteiP33173.

Expressioni

Tissue specificityi

Expressed almost exclusively in adult brain tissue (mainly in the cerebellum and cerebrum) within a single type of neuronal cell. Within the neuronal cell levels are concentrated around the axon, with smaller amounts in the perinuclear and synaptic regions.

Gene expression databases

CleanExiMM_KIF1A.

Interactioni

Subunit structurei

Monomer. Interacts with PPFIA1 and PPFIA4 (By similarity).By similarity

GO - Molecular functioni

  • microtubule binding Source: MGI

Protein-protein interaction databases

DIPiDIP-46956N.
IntActiP33173. 1 interaction.
STRINGi10090.ENSMUSP00000128432.

Structurei

Secondary structure

1
1695
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Helixi17 – 215Combined sources
Beta strandi28 – 314Combined sources
Beta strandi34 – 374Combined sources
Beta strandi40 – 423Combined sources
Beta strandi48 – 514Combined sources
Beta strandi53 – 575Combined sources
Beta strandi64 – 663Combined sources
Helixi70 – 767Combined sources
Helixi78 – 869Combined sources
Beta strandi91 – 966Combined sources
Helixi103 – 1075Combined sources
Helixi112 – 1143Combined sources
Helixi118 – 13114Combined sources
Beta strandi138 – 15013Combined sources
Beta strandi153 – 1564Combined sources
Turni160 – 1623Combined sources
Beta strandi168 – 1714Combined sources
Turni172 – 1743Combined sources
Beta strandi175 – 1784Combined sources
Beta strandi184 – 1863Combined sources
Helixi189 – 20315Combined sources
Helixi206 – 2094Combined sources
Turni210 – 2123Combined sources
Helixi213 – 2164Combined sources
Beta strandi217 – 23014Combined sources
Turni232 – 2354Combined sources
Beta strandi237 – 24812Combined sources
Helixi252 – 2543Combined sources
Helixi265 – 28824Combined sources
Helixi306 – 3083Combined sources
Helixi310 – 3145Combined sources
Helixi316 – 3183Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi324 – 3318Combined sources
Helixi335 – 3373Combined sources
Helixi338 – 35013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I5SX-ray2.20A1-355[»]
1I6IX-ray2.00A1-355[»]
1IA0electron microscopy15.00K1-355[»]
1VFVX-ray1.85A1-355[»]
1VFWX-ray2.30A1-355[»]
1VFXX-ray2.55A1-355[»]
1VFZX-ray2.24A1-355[»]
2HXFelectron microscopy10.00C3-355[»]
2HXHelectron microscopy11.00C3-355[»]
2ZFIX-ray1.55A1-355[»]
2ZFJX-ray3.20A1-355[»]
2ZFKX-ray3.61A1-355[»]
2ZFLX-ray2.70A1-355[»]
2ZFMX-ray2.31A1-355[»]
ProteinModelPortaliP33173.
SMRiP33173. Positions 4-353, 430-605.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33173.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 354350Kinesin motorPROSITE-ProRule annotationAdd
BLAST
Domaini516 – 57257FHAPROSITE-ProRule annotationAdd
BLAST
Domaini1580 – 167899PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili366 – 38318Sequence analysisAdd
BLAST
Coiled coili429 – 46234Sequence analysisAdd
BLAST
Coiled coili622 – 68160Sequence analysisAdd
BLAST
Coiled coili801 – 82222Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Unc-104 subfamily.PROSITE-ProRule annotation
Contains 1 FHA domain.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0245. Eukaryota.
COG5059. LUCA.
HOVERGENiHBG052251.
InParanoidiP33173.
PhylomeDBiP33173.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR022164. Kinesin-like.
IPR027640. Kinesin-like_fam.
IPR022140. Kinesin-like_KIF1-typ.
IPR032405. Kinesin_assoc.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 2 hits.
PfamiPF12473. DUF3694. 1 hit.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
PF16183. Kinesin_assoc. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKETPKSF
60 70 80 90 100
SFDYSYWSHT SPEDINYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG
110 120 130 140 150
AGKSYTMMGK QEKDQQGIIP QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY
160 170 180 190 200
CERVRDLLNP KNKGNLRVRE HPLLGPYVED LSKLAVTSYN DIQDLMDSGN
210 220 230 240 250
KPRTVAATNM NETSSRSHAV FNIIFTQKRH DAETNITTEK VSKISLVDLA
260 270 280 290 300
GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
310 320 330 340 350
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR
360 370 380 390 400
AKQIRCNAII NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD ITDMTNALVG
410 420 430 440 450
MSPSSSLSAL SSRAASVSSL HERILFAPGS EEAIERLKET EKIIAELNET
460 470 480 490 500
WEEKLRRTEA IRMEREALLA EMGVAMREDG GTLGVFSPKK TPHLVNLNED
510 520 530 540 550
PLMSECLLYY IKDGVTRVGR EDAERRQDIV LSGHFIKEEH CIFRSDSRGG
560 570 580 590 600
GEAVVTLEPC EGADTYVNGK KVTEPSILRS GNRIIMGKSH VFRFNHPEQA
610 620 630 640 650
RQERERTPCA ETPAEPVDWA FAQRELLEKQ GIDMKQEMEQ RLQELEDQYR
660 670 680 690 700
REREEATYLL EQQRLDYESK LEALQKQMDS RYYPEVNEEE EEPEDEVQWT
710 720 730 740 750
ERECELALWA FRKWKWYQFT SLRDLLWGNA IFLKEANAIS VELKKKVQFQ
760 770 780 790 800
FVLLTDTLYS PLPPDLLPPE AAKDRETRPF PRTIVAVEVQ DQKNGATHYW
810 820 830 840 850
TLEKLRQRLD LMREMYDRAA EVPSSVVEDC DNVVTGGDPF YDRFPWFRLV
860 870 880 890 900
GRAFVYLSNL LYPVPLVHRV AIVSEKGEVK GFLRVAVQAI SADEEAPDYG
910 920 930 940 950
SGVRQSGTAK ISFDDQHFEK FQSESCPVVG MSRSGTSQEE LRIVEGQGQG
960 970 980 990 1000
ADAGPSADEV NNNTCSAVPP EGLMDSPEKA ALDGPLDTAL DHLRLGSTFT
1010 1020 1030 1040 1050
FRVTVLQASS ISAEYADIFC QFNFIHRHDE AFSTEPLKNT GRGPPLGFYH
1060 1070 1080 1090 1100
VQNIAVEVTK SFIEYIKSQP IVFEVFGHYQ QHPFPPLCKD VLSPLRPSRR
1110 1120 1130 1140 1150
HFPRVMPLSK PVPATKLSTM TRPSPGPCHC KYDLLVYFEI CELEANGDYI
1160 1170 1180 1190 1200
PAVVDHRGAC MGTFLLHQGI QRRITVTLLH ETGSHIRWKE VRELVVGRIR
1210 1220 1230 1240 1250
NTPETDEALI DPNILSLNIL SSGYVHPAQD DRVFFGNDTR TFYQFEAAWD
1260 1270 1280 1290 1300
SSMHNSLLLN RVTPYREKIY MTLSAYIEME NCTQPAVITK DFCMVFYSRD
1310 1320 1330 1340 1350
AKLPASRSIR NLFGSGSLRA TEGNRVTGVY ELSLCHVADA GSPGMQRRRR
1360 1370 1380 1390 1400
RVLDTSVAYV RGEENLAGWR PRSDSLILDH QWELEKLSLL QEVEKTRHYL
1410 1420 1430 1440 1450
LLREKLETTQ RPGPEVLSPA SSEDSESRSS SGASSPLSAE GQPSPLEAPN
1460 1470 1480 1490 1500
ERQRELAVKC LRLLMHTFNR EYTHSHVCIS ASESKLSEMS VTLMRDPSMS
1510 1520 1530 1540 1550
PLGAATLTPS STCPSLIEGR YGATDVRTPQ PCSRPASPEP ELLPELDSKK
1560 1570 1580 1590 1600
TPSPVRATET EKEPQRLLVP DIQEIRVSPI VSKKGYLHFL EPHTAGWAKR
1610 1620 1630 1640 1650
FVVVRRPYAY MYNSDKDTVE RFVLNLSTAQ VEYSEDQQAM LKTPNTFAVC
1660 1670 1680 1690
TEHRGILLQA NSDKDMHDWL YAFNPLLAGT IRSKLSRRRS AQMRV
Length:1,695
Mass (Da):191,725
Last modified:November 1, 1997 - v2
Checksum:iD6EC3B88CBC9CCC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29951 mRNA. Translation: BAA06221.1.
PIRiA56921.
E44259.
UniGeneiMm.276408.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29951 mRNA. Translation: BAA06221.1.
PIRiA56921.
E44259.
UniGeneiMm.276408.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I5SX-ray2.20A1-355[»]
1I6IX-ray2.00A1-355[»]
1IA0electron microscopy15.00K1-355[»]
1VFVX-ray1.85A1-355[»]
1VFWX-ray2.30A1-355[»]
1VFXX-ray2.55A1-355[»]
1VFZX-ray2.24A1-355[»]
2HXFelectron microscopy10.00C3-355[»]
2HXHelectron microscopy11.00C3-355[»]
2ZFIX-ray1.55A1-355[»]
2ZFJX-ray3.20A1-355[»]
2ZFKX-ray3.61A1-355[»]
2ZFLX-ray2.70A1-355[»]
2ZFMX-ray2.31A1-355[»]
ProteinModelPortaliP33173.
SMRiP33173. Positions 4-353, 430-605.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46956N.
IntActiP33173. 1 interaction.
STRINGi10090.ENSMUSP00000128432.

PTM databases

iPTMnetiP33173.
PhosphoSiteiP33173.

Proteomic databases

EPDiP33173.
MaxQBiP33173.
PaxDbiP33173.
PRIDEiP33173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:108391. Kif1a.

Phylogenomic databases

eggNOGiKOG0245. Eukaryota.
COG5059. LUCA.
HOVERGENiHBG052251.
InParanoidiP33173.
PhylomeDBiP33173.

Miscellaneous databases

ChiTaRSiKif1a. mouse.
EvolutionaryTraceiP33173.
PROiP33173.
SOURCEiSearch...

Gene expression databases

CleanExiMM_KIF1A.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR022164. Kinesin-like.
IPR027640. Kinesin-like_fam.
IPR022140. Kinesin-like_KIF1-typ.
IPR032405. Kinesin_assoc.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 2 hits.
PfamiPF12473. DUF3694. 1 hit.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
PF16183. Kinesin_assoc. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The neuron-specific kinesin superfamily protein KIF1A is a unique monomeric motor for anterograde axonal transport of synaptic vesicle precursors."
    Okada Y., Yamazaki H., Sekine-Aizawa Y., Hirokawa N.
    Cell 81:769-780(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 100-247.
    Tissue: Brain.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-612; SER-932; SER-1342; THR-1524; THR-1528; SER-1533 AND SER-1537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-355 IN COMPLEX WITH ADP.
  5. "KIF1A alternately uses two loops to bind microtubules."
    Nitta R., Kikkawa M., Okada Y., Hirokawa N.
    Science 305:678-683(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-355 IN COMPLEX WITH TRANSITION STATE ANALOGS.
  6. "Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin."
    Nitta R., Okada Y., Hirokawa N.
    Nat. Struct. Mol. Biol. 15:1067-1075(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-355 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiKIF1A_MOUSE
AccessioniPrimary (citable) accession number: P33173
Secondary accession number(s): Q61770
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.