ID A0A1S3LDS2_SALSA Unreviewed; 1134 AA.
AC A0A1S3LDS2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3-like isoform X4 {ECO:0000313|RefSeq:XP_013988980.1};
GN Name=LOC106565872 {ECO:0000313|RefSeq:XP_013988980.1};
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_013988980.1};
RN [1] {ECO:0000313|RefSeq:XP_013988980.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013988980.1};
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_013988980.1; XM_014133505.1.
DR AlphaFoldDB; A0A1S3LDS2; -.
DR OrthoDB; 2902917at2759; -.
DR Proteomes; UP000087266; Chromosome ssa12.
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; cd00987; PDZ_serine_protease; 1.
DR CDD; cd00992; PDZ_signaling; 5.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.30.42.10; -; 5.
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; 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:SF65; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 3 ISOFORM X1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 4.
DR Pfam; PF00397; WW; 2.
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; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|RefSeq:XP_013988980.1};
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_013988980.1}.
FT DOMAIN 65..103
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 111..187
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 287..320
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 343..376
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 419..488
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 590..653
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 740..827
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 869..956
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1029..1111
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 217..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 124488 MW; 4B0BD4DE8843277D CRC64;
MSRTLKKKKH WSSKVQECAV SWGSLGEFGN VVEVLGGAEH GEFPYLGQMK LDVMLCHVGT
MPYFGDVLLE INGTPVSGLT NRDTHAVIRH FREPIRLKTV KPGKVLNTDL RHYLSLQFQK
GSLDHKLQQV IRDNLYLRTI PCTTRLPRER EVPGVDYNFI SVGDFRILEE SGLLLESGTY
DGNYYGTPKP PAEPTLVQPD LVDQVLFDED YDNEVQRKRT TSVSKMDRKD SVVPEEEDDD
ERPPLANGLP EHKEGASWRK AVPSYTQSSS AMDFRMWSSL PGDDSLEPLP LNWEMAYTET
GMVYFIDHNS KTTTWLDPRL AKKAKPPEKC EDGGKASGPL QASELPYGWE EIEDPQYGTY
YVDHINQRTQ FENPVLEAKR KLSQETTVSI QQGAPPPPGE GGASGFTPDP SQLQGEMFHT
ALRKSSQGFG FTIIGGDRHD EFLQVKNVLS DSPAAHDNKI SSGDVIVEIN GKCVLGKTHP
EVVQMFQSIP VSQYVDMVLC RGYLLPPDVA GDTENPPPPP PPLQGGEVVT AVPLINGQPL
LVKGDVLHGS SQELHYVTTD ASGRPMVAAL PNGRLSEQGG TGLLQPELVS VPLVKGPGGF
GFAIADCPLG QKVKMILDAQ WCRGLLKGDV IKEINRQNVQ TLSHAQVVDI LKDLQVGSEV
IVLVLRGGQT SPVKSLKPRQ EMTSSTETLD CVTDSVPQAL PYISNTSTLR NNSPKRDTTE
MYLKSKALLE SKQPHTKDLD VFIKRDQETG FGFRVLGGEG PEQPVSTEVY IGAIVHLGAA
EKDGRLRAGD ELIGIDGIMV KGRSHKQVLD LMTNAARNGQ VMLTVRRKVI YRDMTEEEAG
LHMAPVLVNG SPRLPRIQMP SVLDHESFDI TLHRKDSEGF GFVILTSKSK PPLGVIPHKI
GRIIEGSPTD RCGLLNVGDR ISAVNGRSIV GLSHNDIVQL IKDAGNAVTL TVVPEDEYKG
PPSGASSAKQ SPAPHHRAMG QRSAMHDERY NLDLEEEKRE GVTWADYKTL PLSEQGTMCV
TGPKQGCITV ELDRGSRGFG FSLRGGTEYN MGLYILRLAE EGPALLDSRI HVGDQVVEIN
GEPTQGITHT RAIELIQAGG SKVQLLLRPG QGLVQDNSDC VPSTVCYYSN EHHH
//
