ID A0A3Q3RNC5_9TELE Unreviewed; 1458 AA.
AC A0A3Q3RNC5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 {ECO:0000256|ARBA:ARBA00016171};
DE AltName: Full=Membrane-associated guanylate kinase inverted 3 {ECO:0000256|ARBA:ARBA00033438};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000005450.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000005450.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR STRING; 205130.ENSMAMP00000005450; -.
DR Ensembl; ENSMAMT00000005604.2; ENSMAMP00000005450.1; ENSMAMG00000003647.2.
DR GeneTree; ENSGT00940000156496; -.
DR InParanoid; A0A3Q3RNC5; -.
DR OrthoDB; 2902917at2759; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; -; 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:SF10; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 3; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
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 285..318
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 331..364
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 409..478
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 586..649
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 764..847
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 901..988
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1049..1131
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 216..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1458 AA; 160154 MW; D025EF857BDDE872 CRC64;
MSKTLKKKKH WSTKVQECTV SWGGSGELIA VAEVRGGAEM GEFPYLGHIV SEAMVCHAGR
LPSSGDVLLE VNGTPVSGLT NRDTLAVIRH FREPIRLKTV KPGKVLNTDL RHYLSLQFQK
GSLDHKLQQV IRDNLYLRTI PCTTRQPREG EVPGVDYNFI SVGEFRELEE SGLLLESGTY
DGNYYGTPKP PAEPSPVQPD LVDQVLFDEE FDTEVQRKRT TSVSKMDRKD SAAPEEEEDE
EKPPIVNGLT EHKDKAEWKK TVPSYNQSAG AMDLRVWSTH DDSQEPLPKN WEMAYTETGM
VYFIDHNSKT TTWLDPRLAK KSKPPEKCED GELPYGWEKI EDPQYGTYYV DHINQKTQFE
NPVLEAKRKL SVDTPTAVPP PAATPSEEPG KGVRGFTRDP SQLQGSILQT ALRKSPQGFG
FTIIGGDRPD EFLQVKNVLP DGPAAHDNKI ASGDVIVDIN GMCVLGKTHA DVVQMFQSIP
VNQYVDMILC RGYPLPEDSN SSEEVSGGLS TSKDTSPTPS TSTPQDSHYT IPDGGTLSRQ
TAAVPPMTNG GRHHHHLHSH QYHHHLSHVH NQEGPDPTLL QPELVSVPLV KGPGGFGFAI
ADCPLGQKVK MILDAQWCRG LLKGDVIKEI NRQNVQTLSH SQVVDILKDL PVGSEVNVLV
LRGGQTSPVK SLKPCTAPMS QAMSQPTPQQ VVHPIPQQQP QPLTQRQEII NNTETLGQPE
VPSNPLSFST NTLRSSSPKP DASELYLKSK ALLDSKPPNT KDLDVFIKRN QESGFGFRVL
GGEGPDQPVY IGAIVPLGAA EKDGRLRAGD ELLCIDGIPV KGKSHKQVLE LMTNAARNGQ
VMLTVRRKLI HSDDDGDGEE ESDQQPEQVA SLQINSSPKM PRGELPNTIQ PAQFSRPECF
DVTLQRKDNE GFGFVILTSK NKPPPGVIPH KIGRIIEGSP TDRIGKMKVG DRISAVNGQS
IMELSHNDIV QLIKDAGNSV TLTVVPEDDS APPSGTNSAK QSPSAQHRAV GQQPPSYPDR
NSDNEMKNSF PQREMGTLTT TGPKQGCFVV ELERSQRGFG FSLRGGKEYN MGLFILRLAE
DGPALKDGRI HVGDQIVEIN GEATQGITHT RAIELIQAGG NRVHLLLRPG QGLVPDHSSK
DKVTIPTSSF PRLSAYDGHS SPASPSSVSF STSELSPSSP KISVPDEFSG NDSRASWSPG
TGQANREQLS HHNHMRTTSP ITHTQKTGRS DTKSASPKRA TEGWADHTER SQSPRKAERG
HSGSLDDMSR DRKAQGQRDH HFKREPDPAV PLKELEKPQS PRRPAGQQPS TAYGEGKDWK
YMEDDGAYWQ EKGATESIDK SWGTSERHRK GKRAEQEPGA QKSYSEMHRE RAGSDADSGT
QSRKSGRVKG DREYWENKYL GPAEEMNQKD PRGSSSSMHE PTCNGTTTSK KPPITPGPWK
IPSSTKIQSQ VDTAYADV
//
