ID A0A1S3MIW9_SALSA Unreviewed; 1411 AA.
AC A0A1S3MIW9;
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=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2-like isoform X1 {ECO:0000313|RefSeq:XP_014003142.1};
GN Name=LOC106573044 {ECO:0000313|RefSeq:XP_014003142.1};
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_014003142.1};
RN [1] {ECO:0000313|RefSeq:XP_014003142.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014003142.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR RefSeq; XP_014003142.1; XM_014147667.1.
DR KEGG; sasa:106573044; -.
DR OrthoDB; 2902917at2759; -.
DR Proteomes; UP000087266; Chromosome ssa16.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 6.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1.
DR PANTHER; PTHR10316:SF78; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 2 ISOFORM X1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF00595; PDZ; 4.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 6.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 6.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|RefSeq:XP_014003142.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Transferase {ECO:0000313|RefSeq:XP_014003142.1}.
FT DOMAIN 17..100
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 108..184
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 312..345
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 441..510
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 635..700
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 800..890
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 951..1041
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1235..1317
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 178..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1411 AA; 153763 MW; 62188AB6337D6374 CRC64;
MSKSLTKKNH WTNKVHEAVV TRSIEGEFGF ELKGGAEIGQ FPYFGEVKQG KETVQSGKLA
QDELLLEVND TPVAGLTTRD VLAVIKHCKD PIRFKCVKQG GMVDKDLRHY LNLRFSKGSV
DHDHQQIIRD NLYLRTVPCT TRLPKEGEVP GVDYNFVSVE RFMELEQSGA LLESGTYEEN
LYGTPKPPAE PNPAAPPLNV SEALLPGAWP SAQGKRKRNQ SVSNMEQRAS LELPEEEDCS
PPVVNENGVA ITPESSEHED KSTDVSEEVS MMDVLTLPPP FTEPPTEGEE SPEREPPKSP
PKLPKGDEEE LGPLPDNWEM AYTEKEEVYF IDHNTKTTSW LDPRLAKKAK PPEECKEDEL
PYGWEKIDDP IYGSYYVDPV PCSHINRRTQ FENPVQEAKR RLEQQQQMQD QGLSALPLPS
IYREKPQFTR DPTQLKGSFL STALQKSNMG FGFTIIGGDE PDEFLQVKSV IPEGPAAQNQ
KMDTGDVIVY INDICCLGTT HADVVKLFQS VLIGESVTLV LCRGYPLPFD PEDPSGASAG
NSLTPIGMEH HPMVVNGRSS YNHYLEYLSL SSQLPSLAQP GAPHPGDTHL DGSSLPPTNP
GSAPAVTPRD DNVSMVSSGA TGITGGVIQG VELLTVTMVK RAEGFGFTIA DSPTGQRVKQ
VLEPVVQDGV GLNEGDLILE VNQQGVAGAG HGRVVELLKE CPVGAEATLL IQRGGGEGHL
SPWKTSKQIP EQWDPHGSPQ TCLSAPMLPP GTPFSTQPQH RTSVPDSTEG FDLNKPDPYD
LYEKSRAIYE SRRPEYQEVE VHLLREKTGF GFRILGGDEA VQAVSPDARD KIVIGAIIEN
TPAERDGRLR PGDELISVDK MVVAGKPHRY VIDLMHAAAH NGQVSLKVRR RVHFLSEVLG
VNGRSPGYVS TQHNSPPSDV ASASCPITPG NVPPPSTTSP PEGAVPLHTS DVIIHRKENE
GFGFVIISSL NRPENTAVIT VPHKIGRIIE GSPADRCGRL KIDDRILAVN GQSIISMPHA
DIVKLIKDAG LIVTLHIIPE EDPHSRPSSE KQSPMTQKHS PQAQPSPIVN QPSQGASQPG
HAPAQPGQTT TTQEGPAPPA LPSQTPDQPG QVPAAATQPT PGAAAQPSPA GTQQSPVAQP
PGHPPPLYLH DGRSEVKARQ DVKPDIRQPP FTDYRQPPVD YRHPPVADYR QPPTLDYRHP
PPLIDYRQHS TTLAAQFPLA QFPPDFRPQD FDYFTVELEK SVKGFGFSIR GGREYKMDLF
VLRLAEDGPA IRNGRMRVGD QIIEINGDST RDMTHARAIE LIKAGCRRVR LLLKRGTGQV
PEYVDGASPW DTLPPALSAL QEVTLDPHQP PTSSLSSHPA STLDSPHQLS LEASPCTAAQ
APDPSSTRGA TGGRSQTKCT VREQETPHGP G
//
