ID A0A1S3SMX8_SALSA Unreviewed; 1548 AA.
AC A0A1S3SMX8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Kinesin-like protein KIF13B isoform X3 {ECO:0000313|RefSeq:XP_014065693.1};
GN Name=LOC106610714 {ECO:0000313|RefSeq:XP_014065693.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014065693.1};
RN [1] {ECO:0000313|RefSeq:XP_014065693.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014065693.1};
RG RefSeq;
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 RefSeq; XP_014065693.1; XM_014210218.1.
DR GeneID; 106610714; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
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; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
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:SF5; -; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
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; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 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 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:UP000087266}.
FT DOMAIN 10..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 550..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..415
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 622..649
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 552..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1548 AA; 173594 MW; B0487A24DDB7CB29 CRC64;
MGDTSLNDSN VKVAVRVRPM NRREKDLNTK CIVDMEGNQT ILHPGGGNLG KGDSRNQTKT
FAYDYCFWSM DESEKDKFAG QDVVFQCLGE SLLHNAFQGY NACIFAYGQT GSGKSYTMMG
SVDSPGLIPR LCSSLFDRTL LEQREGEGFT IEVSYMEIYN EKVRDLLDPK GSRQALRVRE
HKVLGPYVDG LSRLAVASYK DIESLMSEGN KSRTVAATNM NEESSRSHAV FNIILTHTLK
DLQSGTSGEK VSKLSLVDLA GSERAAKTGA TGERMKEGSN INKSLTTLGL VISALAEQGC
GKNKTKFVPY RDSVLTWLLK DSLGGNSRTA MVATVSPAAD NYDETLSTLR YADRAKSIVN
HAVVNEDPNA RIIRELREEV EKLRDQLTQA ESMKAPELKE RLEESEKLIQ EMTVTWEEKL
RKTEEIAQER QKQLESLGIS LQSSGIRVGE DKCFLVNLNA DPALNELLVY YLKEHTKVGS
ADSQDIQLCG MGIQAEHCII NITTDQWVVL TPHRNSRTCV NGSPCTSPQR LHHGDRILWG
NNHFFRINLP KRRSRGGGEE EEGEGGPMKN SSSSEQLEGD GDTNSEGSSE VSFSYEFAQT
EVMMKALGNN DPMQAVLQSL ERQHEEEKRS ALERQRLMYE QELQQLRRRL HPDRQSVGQA
GTAPSQSQGQ ADRPGQPHYR SLERLSMGGM SNSPSAQSRL RQWSEEREAV LTRSLRKLRE
QIVRANLLVQ EAGFIAEELD KRTEYRVTLQ IPAANLNANR KRDAVLSEPA VQVRRKGKGK
QIWALEKMEN RMVDMRELYQ EWKDYDDDNP VMRSYFKRAD PFFDEQENHS LIGVANVFLS
CLFYDVKLQY AVPIINQKGE VVGRLHVEVV RVAGGVEDSM AGGEDNEASP DGEVQERKLV
CMIKILQATG LPQYLSNYVF CQYSFWDQAE PVIVAPEVDP SASSHSSKEP HCMVVFDSCK
ELGVAVTEEF IEYLTEGALA IEVYGHRQAD SGRNPALWDL SIIQAKTRTL RDRWSEVTRR
LEMWIQVLEI NENGDFMPVE VIPARDVRTG GIFQLRQGQS RRLQVEVRSV QDSGTMPLIA
EVLLAVSVGC VEIRQTHQAK ASNEPIQVEG DEMDSYQERD LERLRHQWLT ALTKRQEYLD
QHLQTLVSKP EKTEEDMERE AQLLEWRLTL TEERNAVMVP SAGSGIPGAP AEWVPLPGME
THTPVLFLDL SADDFSSQEA LEVPEAGGWD ATLSGEDEDD FFDLQIVKHY DGEVKAEASW
DSTVHECPQL SRGGAWPEQR VYLTVRCVVQ LSHPADMQLV LRKRICVNLN PGRQGFAQNL
LKRMSTRSTI PGCGVTFEVV SNIPGDAQGS EDREMLARLA ASAENPKSAD NEAAIEKYLR
SVLAVENILT LDRLRQEVAV KEHLAGKGKG NRRSLSSPSV HRLSGSRQDL SSTCNLENKS
RWESQQDIFI TSPQFSRTLP RPSPPTTPPQ NQDSEQGRSG LAASYLSVKA LVPQMPKLLK
SLFPAREDKK EPLRPSPHSL QHMPRIIMQT TGPEDSRIRI EPVRTTAP
//