ID A0A1S3KLA2_SALSA Unreviewed; 2509 AA.
AC A0A1S3KLA2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Unconventional myosin-IXa-like isoform X8 {ECO:0000313|RefSeq:XP_013979428.1};
GN Name=LOC106560748 {ECO:0000313|RefSeq:XP_013979428.1};
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_013979428.1};
RN [1] {ECO:0000313|RefSeq:XP_013979428.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013979428.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, growth cone
CC {ECO:0000256|ARBA:ARBA00004624}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR RefSeq; XP_013979428.1; XM_014123953.1.
DR GeneID; 106560748; -.
DR CTD; 562199; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd20883; C1_Myosin-IXa; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF3; UNCONVENTIONAL MYOSIN-IXA; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 74..175
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 211..1078
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1971..2020
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 2035..2223
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 960..982
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1224..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1652..1811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2267..2322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2347..2497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2389..2403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2406..2444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2475..2491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2509 AA; 283710 MW; B253F40B60120BDA CRC64;
MPVTLQVKGW NVLSQSPGPR EELPAAAAAA SADGTCCSSM SLQDAGCGYA STNANANVAA
NTASGSMRRR LEDQEFTLRV YPGALAEGTI YCPVGARKST TAAEAIERLL ERLSLDGTKC
YVLAEVKEFG GEEWILNPSD CPVQRMMLWP RNALENRCGL GSGEDYRFLL REKNLDGSIH
YGGSLQMWLL VTEERRRMVE RGFLPQPAGG EHPSDLCALP ELTERALLES LRARFRQEKI
YTYVGSILIV INPFQFLPIY NPKYVKMYDN HALGKLEPHI YAVADVAYHA MLQRRRNQCI
VISGESGSGK TQSTNFLIHH LTALSQKGFA SGVEQIILGA GPVLEAFGNA KTAHNNNSSR
FGKFIQVNYQ ESGTVRGAYV EKYLLEKSRL VYQEHNERNY HVFYYLLAGA SEEERKTFHL
LKPEEYHYLN QMTKKSHRLH WENYYESELQ DCFTVEGEDL KHDFERLQLA MEMVGFLPAT
RKQIFSLLSA ILHLGNIRYR KKSYRDDSID ICNPEVLPTV SELLEVKEEM LFEALTTRKT
VTVGERLIVP YKLAEAGTVR DSMAKSLYSA LFDWIVFRTN HALLNNKDLE DSAKILSIGV
LDIFGFEDYE NNSFEQFCIN FANERLQHYF NQHIFKLEQE EYRAEGISWH NIDYIDNTGC
INLISKKPTA LLHLLDEECN FPQASNQTLL DKFKRQHEGN SYIEFPAVME PAFIIHHYAG
KVKYGVKDFR EKNTDHMRPD IVALLKSSKN AFICGLMGID PVATFRWAVL RAYFRAMVAF
REAGKRHTDK KTGNDAAVPC VVKSVDSFSF LHHPVHQRSL EILQRCKEEK YSITRKNPRT
PLSDLHGTNT LNEKSARDGY GVGCNGRSSI QGRLSSSGSE FDDGVFVNST SSKLLERAQG
ILMRNKNYKS KPCLPKHLLD VKSLRYLSSV TLHDRITKSL LHLHKKKKPP SISAQFQASL
NKLMETLGHS EPYFVKCIRS NAEKLPLRFN DALVLRQLRY TGMLETVRIR QSGYSIKYTF
QDFVRHFRVL LPDSTRPTKS GIREFFGQVH LAPAGYQVGN TMVFLREAER QRLQALLHKE
VLRCIATLQR RFRARLERKH FIKMKQAADV IQRWWRGCLL RQSEAAVDPA VQEEAAVCLQ
AAWKGYRQRR LFLQWQDSAL IIQRSWRNSS QRRVLAAITV QTAWRAYRER AHNCRTHSAA
TLLQAAGRGY LARLRFTELK EQSMNEKQLL NGQRSPTTEE RTPERTMGLD TDASDEQVHE
INHNHDIQDA STVWPTEDSK ESKSACLVKE EEEGESERSQ SIEEPNCHKT RAKRQSRRMR
ELEQAQFSLE LLKVRTHSTG GTLQEEETPV PPCPDSTPCP LDDHQPSSPH RGFPVSHGSF
ELLDTTVDVE AGRQGYPGCH DNQSTPLRTS SQEDLNGPIS PESQPQPQKD PEVVNENDPS
PRVEELPPMI PSPIKEVVAE DPQATFYIPS EDQSSEPKQE SPGKPVKERR ESALRRPVVV
VISMQKETPL EGELQAAPVQ EIALQTGGTT TTSRLTPIAG LEVSEKTQPP RTVTQPWRDL
AGVDRSSLVP SSTSTHGLCP SEVDIQIVPE PKAPSGEVLP NQVERKAGWP VQDNWVSTNS
ILESREVSSK AAAKAPQKKS PTQTIIVSMT EKPPTNTTFC SRRKLPFSKS DKDLVNQERS
LAMQRQEASA SRATAGQRTK EASHKEDHKK FHKTMSSGDL GKVAALGKTS SQDGSRVRGK
MRFWGKAKHA EKKLSREKQQ TIRSESTQGD GTDKTDGTSS PPHSPDLTVT RGRDSKENKD
PSPKVRRRRS VKISSVALEP AQWQNDALHI LTSAHDYRSM NDFLMKKIND LDSEDGKKDT
LVDVVFKKAL KEFRLNIFNS YSTALAMDDG KSIRYKDLYA LFEHILEKSM RLEQRDWSES
PVKVWVNTFK VFLDEFMTEY KPMDSTIGKA PKPERKKRRK KEPDIVEEHN GHIFKSTQYS
IPTYCEYCSS LIWMMDRACV CKLCRYACHR KCCSRMTTKC SKKYDPELSS RQFGVELSRL
TSEERTVPLV VEKLINYIEM HGLYTEGIFR KSGSTNKIKE LRQGLDTDVS SMNLDDYNIH
VIASVLKQWL RDLPNPLMTF ELYEEFLRAM GQPDKREVIR GVYSVIDQLS RTHLSTLERL
IFHLVRITLQ EDTNRMSANA LAIVFAPCIL RCPDTIDPLQ SVQDIGKTTA CVELIIGEQM
NKYRARLKDI NSLEFAENKA KSRLTHIRRS MKPVLIAVRF IGITRTTTPG KGGLRRGSSH
HTPSPPLSPR AHPVVDGDSA GEEGEEPGLT EQQQAAMQQE ERVLTEQIES LQREKEELTY
EMLMLEPRAS DDETLESEAS IGTADSSENL SMDHEGAASN PSGTYRAQKS EAKSRRGLRR
QPDSVDSVDS ILSTASSSLS SSSIIPPSPN YRFRSSSSGP LLASCSSGLG VPVVQSEGDP
RSTVGVKSRH RLRLSRSSPR EAPEGHRRES DFSSPPQQLV LYGSNEFMV
//
