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Database: UniProt
Entry: A0A2Y9MNM8_DELLE
LinkDB: A0A2Y9MNM8_DELLE
Original site: A0A2Y9MNM8_DELLE 
ID   A0A2Y9MNM8_DELLE        Unreviewed;      1767 AA.
AC   A0A2Y9MNM8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Kinesin-like protein KIF1A isoform X15 {ECO:0000313|RefSeq:XP_022423879.1};
GN   Name=KIF1A {ECO:0000313|RefSeq:XP_022423879.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022423879.1};
RN   [1] {ECO:0000313|RefSeq:XP_022423879.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022423879.1};
RG   RefSeq;
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   RefSeq; XP_022423879.1; XM_022568171.2.
DR   Proteomes; UP000248483; Unplaced.
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   3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          5..354
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          516..572
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          1652..1750
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          875..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1484..1523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1598..1638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          430..457
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          628..662
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        875..889
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..908
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1624..1638
FT                   /note="Basic and acidic 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   1767 AA;  198852 MW;  CF6EB1A863592048 CRC64;
     MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKEMPKSF SFDYSYWSHT
     SPEDMNYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEKDQQGIIP
     QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
     LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETNITTEK
     VSKVSLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
     TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAVI
     NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD IADMTNALVG VSPSSSLSAL SSRAASVSSL
     HERILFAPGS EEAIERLKET EKIIAELNET WEEKLRRTEA IRMEREALLA EMGVAMREDG
     GTLGVFSPKK TPHLVNLNED PLMSECLLYY IKDGITRVGR EGAEKRQDIV LSGHFIKEKH
     CVFRSDSRGG GEAVVTLEPC EGADTYVNGK KVTEPSVLRS GNRIIMGKSH VFRFNHPEQA
     RQERERTPCA ETPAEPVDWA FAQRELLEKQ GIDMKQEMEQ RLQELEDQYR REREEATYLL
     EQQRLDYESK LEALQKQMDS RYYPEVNEEE EGPEDEVQWT ERECELALWA FRKWKWYQFT
     SLRDLLWGNA IFLKEANAIS VELKKKVQFQ FVLLTDTLYS PLPPDLLPPE AAKDRETRPF
     PRTIVAVEVQ DQKNGATHYW TLEKLRQRLD LMREMYDRAA EVPSSVIEDC DNVVTGGDPF
     YDRFPWFRLV GSSVISGCNS YPLLNTCMSE RMAALTPSPA SSSPDSDAAE PAEEQSVGEE
     EDLEDDVFPE RMPCDGRDPF YDRPPLFSVV GRAFVYLSNL LYPVPLVHRV AIVSEKGEVK
     GFLRVAVQAI SADDEAPDYG SGVRQSGTAK ISFDDQHFEK FQSESCPVVG MSRSGTSQEE
     LRIVEGQGQG ADAGPSADEV NNNTCSAVTP EGLLDSPEKA ALDGPLDAAL DHLGLGSTFT
     FRVTVLQASS ISAEYADIFC QFNFIHRHDE AFSTEPLKNT GRGPPLGFYH VQNIAVEVTR
     SFIEYIKSQP IVFEVFGHYQ QHPFPPLCKD VLSPLRPSRR HFPRVMPLSK PVPATKLSTL
     TRPCPGPCHC KYDLLVYFEI CELEANGDYI PAVVDHRGGM PCMGTFLLHQ GIQRRITVTL
     LHETGSHIHW KEVRELVVGR IRNTPETDES LIDPNILSLN ILSSGYIYPA QDDRTFYQFE
     AAWDSSMHNS LLLNRVTPYR EKIYMTLSAY VEMENCTQPA VITKDFCMVF YSRDAKLPAS
     RSIRNLFGSG SLRASESNRV TGVYELSLCH VADTGSPGMQ RRRRRVLDTS VAYVRGEENL
     AGWRPRSDSL ILDHQWELEK LSLLQEVEKT RHYLLLREKL EAAQRPGPEA LPPTPSEGSE
     AHSSPTCPLA AAGRPSSLEA PNERQRELAV KCLRLLTHSF NREYTHSHVC ISASESKLSE
     MSVTLLRDPS MSPLGAATLT PSSTCPSLVE GRYGAAELRT PQPCSRPASP EPEPLLEVDS
     KKSPSPARAT ETDKEPRRLL VPDIQEIRVS PIVSKKGYLH FLEPHTAGWA KRFVVVRRPY
     AYMYNSDKDA VERFVLNLST AHVEYSEDQQ AMLKTPNTFA VCTEHRGILL QASSDKDMHD
     WLYAFNPLLA GTIRSKLSRR RSAQMRV
//
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