ID A0A3B3WW32_9TELE Unreviewed; 1699 AA.
AC A0A3B3WW32;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 1b {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:ENSPMEP00000006985.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000006985.1}
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; ENSPMET00000004884.1; ENSPMEP00000006985.1; ENSPMEG00000008579.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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; 6.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 17..100
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 108..190
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 314..347
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 372..405
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 494..563
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 678..756
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 870..952
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1057..1141
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1209..1291
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 181..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1384
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1412
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1487
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1699 AA; 187272 MW; 4B071C6C921C4F04 CRC64;
MTNPALKKNH WTSRVNECSV GKDTRGDLNV SLRGGAENGE FAYIGQINEN LVFYRDGKLN
EGELLLEVEN LSISGLPLYD VQTLIKNCKS PVKLKTVRPG TKLNKDLKHY LSQRFQKSSP
DHELQQTIRE NLYRHAVPCT TRSPREGEVP GVDYNFLSVE DFLVLEKSGT LLEIGTYEGN
YYGTPKPPVQ PPSGKVISGS SGGDAPLSDG LSGSLPGSQN STPRRAKSYN DMRNAGIGLA
DQQLEDDEDL PDMNSSFTGE SSELDEIPHS ARPYVPRHSD PSYAETTPSP SATTESTQQT
NLHLSHPPPE DPLGPLPDNW EMAYTETGEV YFIDHNTKTT SWLDPRCLDK PQKPLEECED
DEGVHTEELD DLELPHGWEK IDDPVYGVYY VDHINRKTQY ENPLLEAKRR RQLEQQPAQQ
PQPQSQQPPE GERYIREWIE DSALAGAPLA TYAANHETYR DPQTGPPVPN AMGQKRGKPF
FTRNRSELNG TFINTKLKKS RRGFGFTVVG GDEPDEFLQI KSLVLDGPAA LDGKMETGDV
IVSVNDTCVL GYTHAQVVKI FQSIPIGSMV NLELCRGYPL PFDPDDPNTS LVTSVAILDN
KDPIIVNGQE VTSSYDSPSS QGSQSTNGPT NGGPPLNGFP RPHSPSTEVA SDTSSQLGYS
NDVVTLASSI ATQPELITVH MEKGDKGFGF TIADSLGGGG QRVKQIVDYP RCRGLREGDI
IIEVNKRNVQ SMSHNQVVDM LSKLPKGSEV TMLVQRGVAP AKKSPKLDYY DLSPPYRDYA
RMQLSRKDSQ SSSQHSVSSH RSAHTDSPVH SSLAAPLSES GTPPAPSQPL PGLPSQDSQG
DGTTHRKPDP FKIWAQSRSM YEIPDFQEQD IFLWRKDTGF GFRILGGNEP GEPIYIGHIV
KYGAADEDGR LRSGDELICV DGTAVVGKSH QLVVQLMQQA AKQGHVNLTV RRKTNYAAKS
EGDVPPSPAS SHHSSTQAPS LTEDMGKRTP QGSQNSLSTV SSGSGSTSGI GSGGGGGGGG
AGIGGNAVVA AAAATTSSQP PNGTTNSAAV SAVQPYDVEI RRGENEGFGF VIVSSVSRPE
AGTTFGRIIE GSPADRCGKL KVGDRILAVN GNSITNKSHS DIVNLIKEAG NTVTLRIIPG
DESSNASLLT NAEKIATITT THTPQQQAAP EARTNTKPKQ ESYEFNTPPN PPLQPPIQTD
STQDSEFYSV DLERDSKGFG FSLRGGREYN MDLYVLRLAE EGAAVRNGKM RVGDEILEIN
GESTKGMKHA RAIELIKNGG RRVHLVLKRG DGSVPEYDGS PNDISTVDAV TGIQNAPEVS
SLPLNNAPSE SSFPPEPPPH SRSKTEPSRR TNGTGNHGTG RHHRSHHRHH SPSKSKAKKS
TGRNGPKLLK KDNKEKDGHR HRSRHRSPHK GHSRSRSADN TLESRDRGHR RGRSPERRQG
QHSSSNHRHH SPRRSPHRSP YRSYHHSPRR SPYRHRSPPR YHSPTRHRHR SLDPYRYDTP
ERHNEKPMAD EAAMSDIPQP RFPFENSILR DSPALDRLNR DPTLSLPPLR REDRLYRQDS
PLMRTSSMER AYRGDRPLKD FASRDYRDVT LPRVRTPDLD SSYQKYTSLF RGRTPEMLER
DGRLASRGVT PEPRYRARSL ERAISPPRRD DSEDEEDDDI FVASKLREYY STLKSDPPPK
PVIPEPKKTY KDSPKDLSI
//
