ID F1SHW6_PIG Unreviewed; 1785 AA.
AC F1SHW6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Kinesin family member 1A {ECO:0000313|Ensembl:ENSSSCP00000017377.4};
GN Name=KIF1A {ECO:0000313|Ensembl:ENSSSCP00000017377.4};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000017377.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000017377.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000017377.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000017377.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR SMR; F1SHW6; -.
DR PaxDb; 9823-ENSSSCP00000017377; -.
DR PeptideAtlas; F1SHW6; -.
DR Ensembl; ENSSSCT00000017858.5; ENSSSCP00000017377.4; ENSSSCG00000016401.5.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000156474; -.
DR HOGENOM; CLU_001485_10_0_1; -.
DR TreeFam; TF105221; -.
DR Proteomes; UP000008227; Chromosome 15.
DR Bgee; ENSSSCG00000016401; Expressed in prefrontal cortex and 24 other cell types or tissues.
DR ExpressionAtlas; F1SHW6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22726; FHA_KIF1A; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR049779; FHA_KIF1A.
DR InterPro; IPR022164; Kinesin-like.
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; IPR049780; PH_KIFIA_KIFIB.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF2; KINESIN-LIKE PROTEIN KIF1A ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1SHW6};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 5..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 525..581
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1670..1768
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 883..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..466
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 637..671
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 883..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..923
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1528
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:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1785 AA; 200800 MW; B823ADE1215332D9 CRC64;
MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKETPKSF SFDYSYWSHT
SPEDINYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEKDQQGIIP
QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETSVTTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAVI
NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD ITDTNTVPGG PKLTNALVGM SPSSSLSALS
SRAASVSSLH ERILFAPGSE EAIERLKETE KIIAELNETW EEKLRRTEAI RMEREALLAE
MGVAMREDGG TLGVFSPKKT PHLVNLNEDP LMSECLLYYI KDGITRVGRE DAEKRQDIVL
SGHFIKEEHC VFRSDSRGGG EAVVTLEPCE GADTYVNGKK VTEPSVLRSG NRIIMGKSHV
FRFNHPEQAR QERERTPCAE TPSEPVDWAF AQRELLEKQG IDMKQEMEQR LQELEDQYRR
EREEATYLLE QQRLDYESKL EALQKQMDSR YYPEVNEEEE EPEDEVQWTE RECELALWAF
RKWRWYQFTS LRDLLWGNAI FLKEANAISV ELKKKVQFQF VLLTDTLYSP LPPDLLPPEA
ADRETRPFPR TIVAVEVQDQ KNGATHYWTL EKLRQRLDLM REMYDRAAEV PSSVIEDCDN
VVTGGDPFYD RFPWFRLVGS SVVSGCNSYP LLNTCMSERM AALTPSPTFS SPDSDATEPA
EEQSVGEEEE EEEEEEDLED DVFPEHVLCD GRDPFYDRPP LFSLVGRAFV YLSNLLYPVP
LVHRVAIVSE KGEVKGFLRV AVQAISADEE APDYGSGVRQ SGTAKISFDD QHFEKFQSES
CPGAGMSRSG ASQEELRIVE GQGQGADAGP SADEVNNNTC SAVTPEGLLD SPEKATLDGP
LDAALDHLGL GSTFTFRVTV LQASSISAEY ADIFCQFNFI HRHDEAFSTE PLKNTGRGPP
LGFYHVQNIA VEVTRSFIEY IKSQPIVFEV FGHYQQHPFP PLCKDVLSPL RPSRRHFPRV
MPLSKPVPAT KLSALTRHCP GPCHCKYDLL VYFEICELEA NGDYIPAVVD HRGGMPCMGT
FLLHQGIQRR ITVTLLHETG SHIHWKEVRE LVVGRIRNTP ETDESLIDPN ILSLNILSSG
YIYPAQDDRT FYQFEAAWDS SMHNSLLLNR VTPYREKIYM TLSAYIEMEN CTQPAVITKD
FCMVFYSRDA KLPASRSIRN LFGSGSLRAS ESNRVTGVYE LSLCHVADAG SPGTQRRRRR
VLDTSVAYVR GEENLAGWRP RSDSLILDHQ WELEKLSLLQ EVEKTRHYLL LREKLETAQR
PGPEALSPAS SEDSEAHSSS SASSPLAAEG RPSSLEAPNE RQRELAVKCL RLLTHSFNRE
YTHSHVCISA SESKLSEMSV TLLRDPSMSP LGAATLTPSS TCPSLVEGRY GAPDLRTPQP
CSRPASPEPE PLPEADSKKL PSPARGASEA DKETPRLLVP DIQEIRVSPI VSKKGYLHFL
EPHTAGWAKR FVVVRRPYAY MYNSDKDAVE RFVLNLSTAQ VEYSEDQQAM LKTPNTFAVC
TEHRGILLQA NSDKDMHDWL YAFNPLLAGT IRSKLSRRRS AQMRV
//
