ID A0A3B3X6T8_9TELE Unreviewed; 1416 AA.
AC A0A3B3X6T8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 2a {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000010747.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000010747.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR Ensembl; ENSPMET00000017675.1; ENSPMEP00000010747.1; ENSPMEG00000012951.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00992; PDZ_signaling; 6.
DR CDD; cd22541; SP5_N; 1.
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:SF27; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF00595; PDZ; 6.
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; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 18..101
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 164..208
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 324..357
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 370..403
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 449..518
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 641..704
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 742..832
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 895..985
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1135..1217
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 226..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1048
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1416 AA; 154104 MW; 06C552647A9F2A55 CRC64;
MSKTLKKRKN HWTNKVHESI LCRNEEGELG LELKGGAEHG QFPVIGELLP GRAACHSGKL
LQEDLLLEVN DTPVAGLTTR DVHAVVKHSK DPVRLKCVKQ GGVIDKDLRR YLSLRFQKGS
VDHELQQIIR DNLYLRTVPY TSSLRFRHIA METDVMSVLV CRGTTRQPKE GEVPGVDYNF
VTVDRFMELE KSGALLESGT YEENFYGTPK PPAEPSALLL NVTDHLLPGA RPSSEGKRKR
NKSVSNMERA GVEPPEEEEE KPVVNGNGVA VTPESSEHED KSTDASGDVG PQSNPAEAPA
EVPQEDGQSP KTVVPKPEEN DELGPLPDNW EMAYTEKGEV YFIDHNTKTT SWLDPRLAKK
AKPPEECKED ELPYGWEKID DPIYGSYYVD HINRRTQFEN PVLEAKRRLQ QQQQQMQSQG
LSSLPLPAIY REKPLFTRDP TQLKGSFLST ALQKSNMGFG FTIIGGDEPD EFLQVKSVIP
DGPAAADGKM ATGDVIVYIN DVCVLGTTHA DVVKLFQSVP IGQSVTLVLC RGYPLPYDPE
DASNTNNATT TIISPLGIME QRPIMVNGRT GYDNYLDYLT RTARFVTDPS QDHVNSQQPP
LLGAHPGDTH LDGSLPATTG TTPPDSVSMA SSGATQGELL TVTMVKGVDG FGFTIADSLT
GQRVKQVLEP QGCPGLCEGD LILEINKQAV AGFTHTQVVE LLKECAVGAE ASLVVQRGGT
ELVQPRTVFP VDSTGAEYQD IEVHLRRQKS GFGFRVLGGD EAGQPVSVET REKILIGAII
EKSPADLDGR LRPGDELLFV DGIPVVGKAH RYVIDLMHAA GRNGQVNLVI RRRTQAGGES
CPENSRSPGS ASTQHSSPHS DYTYANSTSQ TANSGPGNAS AASDGTSAAN TKPSDVTISR
KESEGFGFVI ISSLNRPETA ATNTVPHKIG RIIEGSPADR SGKLKVGDRI LAVNGQSIVS
MPHADIVKLI KDAGLSVTLR IIPQEELSNP PSATASEKQS PMAQQHSPKV QPNAAPSQSN
PAPVEPHPSA AQPNPAPHHS PVTQLPVPPP QTYTHDSSYR SEVKARQDVK PDIRQPPFTD
YRQPPVDYRH PPVADYRQPP TLDYRHPPLL DYRPFAIPDY RMPPVQLSQD FDYFTVELEK
SVKGFGFSIR GGREYKMDLF VLRLAEDGPA IRNGRMRVGD QIIEINGEST RDMTHARAIE
LIKAGGRRVR LLLKRGTGQV PEYDNAAPWD GRPSASPSLS EVGPPTDSLS MPTPSSHLAP
APDPPHLPPL DAARDTSRTE RSKSPQKAEL LLNRDAMSQG RRIAKSNGGR STHKGHRLQQ
QQHTTEGDGD KEGQGGESKP VRSTRGRSKE RTHSPGGSKI PHTNGNSRES AERRGKSSSS
TTGVGRKATV SPGPWKIPGS DKLPSTLRAG ASTLSR
//
