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Database: UniProt
Entry: A0A3Q1AN24_AMPOC
LinkDB: A0A3Q1AN24_AMPOC
Original site: A0A3Q1AN24_AMPOC 
ID   A0A3Q1AN24_AMPOC        Unreviewed;      1687 AA.
AC   A0A3Q1AN24;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Kinesin-like protein KIF13B {ECO:0000313|Ensembl:ENSAOCP00000002129.1};
GN   Name=KIF13B {ECO:0000313|Ensembl:ENSAOCP00000002129.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000002129.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000002129.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   Ensembl; ENSAOCT00000012049.1; ENSAOCP00000002129.1; ENSAOCG00000005286.1.
DR   GeneTree; ENSGT00940000155500; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; 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   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
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; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12473; DUF3694; 2.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|SAM:Phobius};
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:UP000257160};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..345
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1585..1627
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          1401..1422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1449..1493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1632..1687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          357..402
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1471..1493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         95..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1687 AA;  187756 MW;  C2D15010877AE819 CRC64;
     MSSFKYQLLT VILSFLFSFA SRTQPKVRFT LNFHFLVSLQ LILVIFVFAY DYCFWSMDES
     QKDKFAGQDV VFQCLGENLL DNAFMGYNAC IFAYGQTGSG KSYTMMGSAE QPGLIPRLSS
     SLFSRTVQEA REGESFTVEV SYMEIYNEKV RDLLDPKGSR QALRVREHKV LGPYVDGLSH
     LAVASYKDIE SLMSEGNKSR TVAATNMNEE SSRSHAVFNI ILTHTLMDLQ SGTSGEKVSK
     LSLVDLAGSE RAAKTGAAGE RLKEGSNINK SLSTLGLVIS ALAEQGAGKN KSKFVPYRDS
     VLTWLLKDSL GGNSRTAMVA TISPAADNYD ETLSTLRYAD RAKSIVNHAV VNEDPNARII
     RELREEVEKL REQLTEAESM KAPELKERLE ESEKLIQEMM VTWEDKLRKT EAIAQERQKQ
     LESLGISLQS SGIRVVDDKC FLVNLNADPA LNELLVYYLK DHTRVGSADS QDIQLCGMAI
     QPEHCIIDVL ENNGVMLSPH RNARTCVNGS AVSCPVQLHH GDRILWGNNH FFRSVLVYKL
     RSHEDGGAAV KTCLSSDRLE VDPDAASDVS SELSFGYEFA QAEVMMKGMG NNDPLQSVLQ
     TLERQHEEEK RCALERQRLM YEQELQQLRQ RLSPEKPTLC RTTFVLWCRE AMMTRSLRRL
     REQILRARLL AQEAGFIAEE LNKRTEYLVT LQIPAANLDA NRKRDVVLSE PAIQVRRKGK
     GKQIWALEKM ENRLVDMREL YQEWKDFDED NPVMRSYFKR ADPFFDEQEN HSLIGVANVF
     LACLFYDVKL QYAVPIINQK GEVAGRLHVE VFRGTEIKYN SVPTVSSSSV LQVKVLQATG
     LPRHLSNFVF CQYHFWGQEE PVFTAPEVAP SSSSSASRDP QCTVVFDSEL SVPVSEDFVE
     FLAEGAVAIE VYGHKQANHR RNLALWDLGV IQAKTRSLRE RWSEVTRRLE LWVQVMELNE
     AGEFTPVEVQ PAKDVRTGGT FQLRQGQSRR VQVEVRSVSD SGTMPLIAAS ILSVSIGDVK
     VQQIRHSRND SQWVDLERMR EQWLLTLTQR QEYLDQQLQK IVSKPDKSED DVERESQLLE
     CRLTLTEERN AVLVPSAGSG IPGAPVERVP VPGMETHIPV LFLDLSADDF QSSLSAPLAG
     GLDALLSRED DDDFFDLHIV KHCDPEVKVE ASWDSTVHEC PQLSRVTSAD QRVYLTVRSV
     VQLSHPAHMQ LVLRKRICVN VTGRQGFAQS LLRRMSQRST IPSCGVTFEI VSNIPGDIHG
     PEDREMLARL AASAEDDQSA DSEAAIEKYL RSVLAVENVL TLDRLRQEVA VREQLAVRGK
     AARRCLSSPD IQRVRSLQAD HLSPLSLAQR MTIGVVALTL EAFQIRLQVS NSIVSMVSSQ
     IPTEEVLPST MEPNIPKSVP LPPPIIPETE DSTPSPVSEA SSGYMSTSIS TATLSEVYTL
     SWDLPPSLSS RADGFEAVPD EEEEDSKETQ RSSPLYIASQ SNTGPEPLHD SKSVSSVANP
     FKIQKVMSSD LKSFQQILGE EEGSLGRASS LGTGLNLSVP MESLEIISDT EEGDAAVSAV
     LPDWLKEGEF VTVGANKSGT VRYLGPTDFA EGTWVGVELE VPAGKNDGSV GGKHYFYCNP
     GYGVLVRPDR VTRGGAKRRR QQQQKHRSAN LSGSSPNLAA LTALAKGHAG GASSGRSRGE
     NRKSWNN
//
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