ID A0A2T7PTP0_POMCA Unreviewed; 1831 AA.
AC A0A2T7PTP0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Kinesin-like protein unc-104 {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_03769 {ECO:0000313|EMBL:PVD36779.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD36779.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD36779.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD36779.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD36779.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD36779.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PZQS01000002; PVD36779.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7PTP0; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg2.
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; cd22705; FHA_KIF1; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR CDD; cd22249; UDM1_RNF168_RNF169-like; 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; 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; 2.
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; 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:UP000245119};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 67..422
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1670..1768
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1139..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 683..739
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1149..1163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1831 AA; 208283 MW; A05FCE7437443938 CRC64;
MQILLISKIL PPHPPPTNFS LKGSKGSHLL YSHASLSFYK LQMMSSDLSV FRLPACSAAR
AKARMSSVKV AVRVRPFNSR EMSRDAECII QMGGNTTTIT NPKAGPKEAK TKTFEFDHSY
WSHTDPSDPS FASQKQVYDD IGLEMLDHAF EGYNVCIFAY GQTGAGKSYT MMGRSDPGQQ
GIIPQLCEDL FERIKRQNCD EIQFSVEVSY MEIYCERVRD LLNPSNKNSL RVREHPLLGP
YVEDLSKLAV QSFNDINNLI DEGNKARTVA ATNMNETSSR SHAVFTIIFT QKKFDLDTKM
AGEKVSKISL VDLAGSERAD STGAKGTRLK EGANINKSLT TLGKVISALA EVCKQEKLYG
VAHKRKKKAE FIPYRDSVLT WLLRENLGGN SKTAMVAALS PADINYDETL STLRYADRAK
QIMCKAVVNE DPNARLIREL KDEVSRLREL LAAEGIDIGD MNLQDLHEER ERNRSRKSSV
TIEGEDAIER LKESEKLIAE LNESWEEKLR RTEAIRIERE AVLAEMGVAL REDGGTIGVF
SPKRTAHLVN LNEDPLMSEC LLYYIKDGTT RVGRHDAQNP QDIQLSGTHI LEEHCYFESV
DGTVMLLPCE GAMCYVNGRQ VTEPTALKTG SRVILGKHHV FRFNHPQQGH CFDNEVAVKI
SLNSAKTTAE PVDWTFAQLE LLEKQGIDLR KEMEQRLMNL EEQYRKEKEE ADLLFEQQRQ
DYENRIQTLQ EQVERHSMIS SVATTDFLRE EEEEEEEVKW TDREKELASW GFRKWKYHQF
TSLRDDLWGN AIFLKEANAI SVELNKKVQF QFVLLTDTLY SPLPPDLLPS DHTRGQTDEP
RPFPRTVVAV EVQDTKNGAT HYWSLEKLRQ RLELMREMYH NEAELSPTSP EPTIDTMTGG
DPFYDRFPWF RLVGRAFVYL SNLYYPVPLV HRVAICTGDL MSIIHRSEKE DTPDFSTGIK
QSGNAKITFK DEDYFIKHPQ DASTVPIVTK RADQSQDKVS SQEELRIVEG QGQGMDNSIL
ISEDVNEGAE VDYCPQINVK ELPEHLQLGS QFQFRVTVLQ ASCISPEYAD IFCQFNFLHR
HDEAFSTEPL KNTGKGPPLG FYHVQNFTVC VTKSFIDYIK TQPLVFEVLG HYQQHPLHDQ
ARETPYVRPP PRRSFPSSLP VSKPVPSPKY GLITAPSEND KKSSKARKNR SLILECPKLR
QLCSSPVCSH CDLLVWFEIC ELAHNGEYVP VVVDHSGDMP TRGTFMLHQG IQRRMRITLL
HEKRSDFCWK DVKELVVGRI RNTQEYHDLD SESTVLSLSL FPAHFLQYSN DDRVFFQFEA
AWDSSLHDTP LLNRVTPHGE NVYMTLSAYL EMENCPQPAC VTKDLTLVIH PRDVKISAPR
ALRSLFGGSR SMDCNKVSGV YELLLRKFSE TGSPGVERRQ RRVLDTSSTY VRGEENLNGW
RPRGDSLLVD HQWELEKLTR LQMVEKTRHV LLLREKLLEQ NKTSELSKLD KEIQNSQAKA
RSLHGIPMDA SIYISDENSK DFDMKEKEIQ QTQNIYDLKA IEDHEKQLLA RCARLMLQGK
LPLKPPPIDA IAVSVTDSLL SSSIITTSEE SDSAISDSMG ISMVSSTSDL VKSVTSVPIQ
PSRSCENIQT TGVSPIAETN DRKLSLPLKP INLDAPLFVP DVEEVRVSPV VSRRGYLNFL
EENTNGWMKR WVVVRRPYVY VYNNEKDPVV RAIINLATAH IEYSEDQQAL LKTQNAFSVM
TKTRGFLLQT IDDKDFHDWL YAINPLLAGQ ISRDAEDDRN MCFQVQAVKE EAGYDDLKAI
SCNETEMEKV IEVSESSNCM AGTLCCYKRR R
//
