ID A0A1S3T3T1_SALSA Unreviewed; 1344 AA.
AC A0A1S3T3T1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Kinesin-like protein KIF14 isoform X2 {ECO:0000313|RefSeq:XP_014071232.1};
GN Name=LOC106613482 {ECO:0000313|RefSeq:XP_014071232.1};
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_014071232.1};
RN [1] {ECO:0000313|RefSeq:XP_014071232.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014071232.1};
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}.
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 RefSeq; XP_014071232.1; XM_014215757.1.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd22707; FHA_KIF14; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
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; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
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 347..691
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 59..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 731..783
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 918..1017
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 59..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 436..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1344 AA; 150773 MW; CE1283152FAFBD96 CRC64;
MSLYSISAKK HTAFYDNFLT SRVPDTKNQK PARGMIKGDD TKLVTLDKTK EINTTNFNSA
LSKTGGQRNG TPGRGRLTLQ RKTGTNGDKV MSENTMEVTQ NRTPVPEKRL TLQRRTRTGS
IDKSASNDTS KATESSRQHW VSGTDSHHSK VLSESNPPTP VSAVVLRSFS LRDSSSRSKS
REAVRLLNTP AKGVKLFAPK QPAAPGKVDV TKPEDHTRTF STPTKKTHFE KITAKKDAFE
RLAGKDITKV VAVKMVGLER PKTHAQVTVE AAKPVATPYT NKFLVSSQRA NVTSNLLPGQ
VRKYSIHGDL TMARSSTPVP TSSTELLLPP SAMLKHEQDP LKMENSAVTV AVRMRPFNTR
EKTEKALQVI FMDNQETLVQ HPDTKQSYSF TYDFSFCSVD KSDPGFASQQ TVYEKLAKPL
LERAFEGFNT CLFAYGQTGS GKSYTMMGVG EEAGVTPRFC EELFSRLSVV DNQEVTCHLE
MSYFEVYNEK IHDLLIARNE QNQKRWPLRV REHPVNGPYV AELTTNVVSS YVDIQGWLEL
GNKQRATAAT GMNDKSSRSH SVLTLVMTQT KTEFVEGEEH DHRITSRINL VDLAGSERCS
SAQTSGERLR EGASINKSLL TLGKVISALS EQAQTKRKVF TPYRDSVLTW LLKESLGGNS
KTAMIATLSP AGSNVEESLS TLRYAKQARM IINVAKVNED TNAKLIRELK AEVEKLRAAQ
MSSQGIEPET INLFQQEILA LKSKLTQQER EMAEAHRAWR EKLEQAEKRK REETKELQKA
GITFKVDNRL PNLVNLNEDP QLSEMLLYMI KEGQTKVGQH KSESAHDIQL SGALIADHHC
VISNVNGEVS IIPMENAKTF VNGNLVSETT VLHRGDRVIL GGDHYFRFNH PAEVQSGKSV
SCWTGDGDGH KDFEFAKNEL LSAQRVQLEE EIEAARLKAK EEMMQGIQVA KEMAQKELSD
QKTQYENRIK ALERELEEES ERKRCQAMDQ QRVVSKMEEL QFAKVELEQE VDTHKTRLRL
HMEAQATRQA MADHGVRQAK VVEALEAEKR KIGKDLEEMQ RKVAQKGSQT LKNVPPQWDA
MKLSLMIEEA NKISGKLMKN TVFSRHEGSR KEGGGGKGEL QVQVQNTKLG ISTFWSLEKF
QSNLAAMREL DQGDRSACKD DDVFYDPNDE WEQDVSASST ASSFSRRRSR SLLKSRRISG
RLYEIRVHPI QSLHNSNTSQ SSGLMGVAKP PSLHPSSLDS NLPGICKDFI GQMVGQLRWC
HSYEESMADR LSSDLYCVYT AVTTISGLYD GLDDDCQGSE LRRQSKCPTC FEPHYSVLEL
RSHAKLERWL TTKSSIKLPR CDFS
//
