ID A0A3B5RED1_XIPMA Unreviewed; 1472 AA.
AC A0A3B5RED1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 2 {ECO:0000313|Ensembl:ENSXMAP00000041580.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000041580.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000041580.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000041580.1};
RG Ensembl;
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 Ensembl; ENSXMAT00000037158.1; ENSXMAP00000041580.1; ENSXMAG00000004682.2.
DR GeneTree; ENSGT00940000155057; -.
DR OrthoDB; 2902917at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000002852};
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 109..185
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 304..337
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 350..383
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 428..497
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 620..683
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 801..891
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 954..1044
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1193..1275
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 204..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1472 AA; 160426 MW; 1BDD7FD1C9053786 CRC64;
MSKTLKKRKN HWTNKVHESI LCRNEEGELG LELKGGAERG QFPVIGELLP GKAACHSGKL
LQEDLLLEVN DTPVAGLTTR DVHAVVKHSK DPVRLKCVKQ GGVIDKDLRR YLNLRFQKGS
VDHELQQIIR DNLYLRTVPC TTRQPKEGEV PGVDYNFVTI DQFMELEKSG ALLESGTYEE
NFYGTPKPPA EPSALLLNVT DQLLPGARPS SEGKRKRNKS VSNMERAGVE PPKEEEEEEE
KPVVNGNGVA VTPESSEHED KSTDASGDVG PQSNPAEAPA EVPQEDGQSP KTAVPKPEEN
DELGPLPDNW EMAYTEKGEV YFIDHNTKTT SWLDPRLAKK AKPPEECKED ELPYGWEKID
DPIYGSYYVD HINRRTQFEN PVLEAKRRLQ QQQQMQSQGL SSLPLPAIYR EKPLFTRDPT
QLKGSFLSTA LQKSNMGFGF TIIGGDEPDE FLQVKSVIPD GPAAADGKMA TGDVIVYIND
VCVLGTTHAD VVKLFQSVPI GQSVTLVLCR GYPLPYDPED ASNTNNSTTT IISPLGIMEQ
RPIMVNGRTG YDNYLDYLTR TARFITDPSQ DHVNCQQPPL LTAHPGDTHL DGSLPANTGT
TPPDSVSMAS SGATQGELLT VTMVKGVDGF GFTIADSLTG QRVKQVLEPQ GCPGLCEGDL
ILEINKQAVA GFTHTQVVEL LKECAVGAEA SLVVQRGGTG HYSPWKTPKQ VLEQWEFQQG
QNSPAQTSRS APIVSHSAPF PTHHLHMASV PDSASEALAL VKPDPYDLFE KSMAIYESRQ
PVQPRTVFPL DSTGAEYQDI EVHLRRQKSG FGFRVLGGDE AGQPVSVETR EKILIGAIIE
KSPADLDGRL RPGDELLFVD GIPVVGKAHR YVIDLMHAAG RNGQVNLVIR RRTQAGGESC
PENSRSPGSA STQHSSPHSD YTYANSTSQA ANSGTGNASA TSDGTSAANA KPSDITISRK
ESEGFGFVII SSLNRSEMAA TNTVPHKIGR IIEGSPADRS RKLKVGDRIL AVNGQSIVSM
PHADIVKLIK DAGLSVTLRI IPQEELSNPP SATASEKQSP MAQQHSPKAQ PNTAASQSNP
AAVEPHPSAA QPNPAPHHSP VTQLPVPPQT YTHDGSYRSE VKARQDVKPD IRQPPFTDYR
QPPVDYRHPP VADYRQPPTL DYRHPPLLDY RPFAIPDYRM PPVQLSQDFD YFTVELEKSM
KGFGFSIRGG REYKMDLFVL RLAEDGPAIR NGRMRVGDQI IEINGESTRD MTHARAIELI
KVGGRRVRLL LKRGTGQVPE YDNAVPWDGR PSASPSLSEV GPPTDSLSMP TPSSHLAPAL
DPPHLPPLDA SRDASRTERS KSPQKAELLL NRDAMSQGRR IAKSDGGGST HKGHRLQQHT
TDGDGDKEGQ GGESKPLRST RGRSKERTHS PGGSKIPHTN RNGRESAERR GKSTSSATGA
GRKATVSPGP WKIPGSDKLP STLRAGASTL SR
//
