ID A0A1S3LDI7_SALSA Unreviewed; 1652 AA.
AC A0A1S3LDI7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1-like isoform X6 {ECO:0000313|RefSeq:XP_013988895.1};
GN Name=LOC106565841 {ECO:0000313|RefSeq:XP_013988895.1};
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_013988895.1};
RN [1] {ECO:0000313|RefSeq:XP_013988895.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013988895.1};
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_013988895.1; XM_014133420.1.
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; cd00992; PDZ_signaling; 5.
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; 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:SF12; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF16666; MAGI_u5; 1.
DR Pfam; PF00595; PDZ; 5.
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_013988895.1};
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_013988895.1}.
FT DOMAIN 17..100
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 104..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 359..392
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 472..541
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 646..724
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 824..906
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 988..1084
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1153..1235
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 201..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1302
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1358
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1409
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1652 AA; 181617 MW; F4AE6F810969DD3B CRC64;
MAKVIQKKNH WTTKVNECAV LKDALGDLNV PLLGGAENGE FAYIGQVNED IVIYKNGKLT
EGELILEVEN LSISGLPLYD VQTVINNCKG PIRLKTVRQG TKLNKDLKHY LSQRFLKSSQ
DHELQQTIRD NLYRHAVPCT TRPPRDGEVP GIDYNFLPVE DFLALEQSGT LLEVGAYEGN
YYGTPKPPRQ PPSGKVITRD ALQDSLPGSQ HSTPRRTKSY NEMQNAGIVP VDLEEDEELP
EMNSSLTDNK YFSRNTRLVN TGDSSEPDEH PYAPRENAPS YGVNNTLSST TEDSQQTHIH
LSHPPTEEDP LGPLTDNWEM AYTENGELYF IDHNTKTTSW IDPRCLDKPP KPLEECEDDE
LPTGWEKIDD PVYGVYYVDH INRKTQYENP ILEAKRLKQL EQQQPPEGER YIQEWIEDAT
LAGAPLASYT ANHQETYRDP QAGPPLPPLI GPKRGKPFFT RNPAELKGTF INTKLRKSHR
GFGFTVVGGD EPDEFLQIKS LVLDGPAALD GKMETGDVIV SVNDTCVLGY THAQVVKVFQ
SIHIGSMVNL ELCRGYPLPF DPDDPNTSMV TSVAIVDKEP IIVNGQDSYD SPSSHGSHTG
GPVNGMRESR PHSPSSAEVA SNSSHGYLSD SVTLASSIAT QPELITVHME KGDKGFGFTI
ADSPAGGGQR VKQIVDYPRC RGLKEGDIIV EVNKRNVQSM SHNQVVDLLS KCPKGSEVSM
LVQRGGGVAP AKKSPRLQLA RKDSQNSSVS SHRSTHTDSP VHTSLAPPLS KSSAPPPPSQ
PLPGLPTQDP QADGTVHRKP DPFKIWAQSR SMYESRLPDF QEQDIFLWRK DTGYGFRILG
GNEPGEPIYI GHIVKYGAAD EDGRLRSGDE LICVDGTAVM GKSHQLVVQL MQQAAKQGHV
NLTVRRKTGY GVSKGEGEVP PSPASSHHSS TQAPSLTEGK RTPQGSQNSL NTVSSGSGSG
SGSTSGIGSG GGGGSGSAVV NTALQPYDVE IHRGENEGFG FVIVSSVSRP ESGTTFAGNA
CVAMPHKIGR IIEGSPADRC GKLKVGDRIL AVNGCSITNK SHSDIVNLIK EAGNTVTLRI
IPGDDSSNAS LLTNAEKIAT ITTTHTPQQQ AAPEPRNNTK PKQESSFEFK SPQAPPPPAP
TTQPPAQDAA FYSVDLEREN KGFGFSLRGG HEYNMDLYVL RLAEDGAAVR NGNMSVGDEI
LEINGESTKG MKHARAIELI KDGGRHAHLV LKRGDGSVPE YDPSIDGAGP AAGVQNASEV
STLPHNNTPS DTNTPDPHKP SRSKDKKGHH HSKHRHRSPD KKSKSKGGLS GETGASSNQS
KRKGDKSKRS GGDNHGTHQH HSNSSGHRHR RHRSPDKGRS RARSAEKTLD SRQSQGHRER
EGRSPDRHHT HRQRSPYRSP RRNRSPYGHR SPYAHRSPYG HRSPYRSRHH SPTRYHRTQS
SDPYRQPSPY RLRGQEPERP NVGVAPVLRK PPGPVPSPYR EESVLREPPA LDRLNREATL
LRESREERLF EEDSLLLRAS TLERDYRGDG LLSAAARGQR GETMPRVRTP ESDSAYKRYS
SLLRGRSPER MEREARYAPR EESPDPRYRV RSLGRDISPV RSFIELEEEE GATAPRLKES
YSTLKSDISR ASKAPPEPKR KAYKDSPKDL SI
//
