ID A0A3B4CIU3_PYGNA Unreviewed; 1483 AA.
AC A0A3B4CIU3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1-like {ECO:0000313|Ensembl:ENSPNAP00000010751.1};
GN Name=MAGI1 {ECO:0000313|Ensembl:ENSPNAP00000010751.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000010751.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000010751.1}
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 STRING; 42514.ENSPNAP00000010751; -.
DR Ensembl; ENSPNAT00000017541.1; ENSPNAP00000010751.1; ENSPNAG00000016452.1.
DR GeneTree; ENSGT00940000155820; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00992; PDZ_signaling; 5.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.30.42.10; -; 5.
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:SF77; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 1 ISOFORM X1; 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; 5.
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; 5.
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 92..168
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 280..313
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 327..360
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 422..491
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 595..675
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 757..839
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 920..1016
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1041..1123
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 187..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1483 AA; 162863 MW; 9EDF6F8DC97BE976 CRC64;
MSKVIQKKNH WTTRVNECAV CKSSGGELSV RLRGGAESGE FTYVGEVRED TVEGLSVSGL
PLYDVLTVIK NCKGPVRMKT VRQGHKLNKD LRHYLSLRFQ KSSPDYDLQQ TIRDNLYRHA
VPCTTRPPRD GEVPGVDYNF LSVQEFLELE QCGTLLEIGT YEGNYYGTPK PPNHPSCASV
ITQDALRDGL PGSQNSTPKR TKSYNDMQHA RVVPVEPTED ADFSTDMNNA FTGDSSRQEV
HGVVRDNAPS NALSNVAVSP AATMASSHHP HLPPEDDPLG PLPDNWEMAY TESGEVYFID
HNTKTTSWMD PRCADKQQKP LEECDDDELP PGWEKIDDPV YGVYYVDHIN RKTQYENPVL
EARRKKQVDI QQPPEEWIEE HSSAGAPIAA YVPNHLETYR DPQRGKPFFT RNPAELKGTF
INTKLLKSRR GFGFTVVGGD EPDEFLQIKS LVLDGPAAVD GKMETGDVIV SVNDTIVLGY
THAQVVKIFQ SIPIGSMVQL ELCRGYPLPF DPDDPNTSLV TSVAILDKEP IIVNGQEAFD
PPPLGLSQSA TGPTEPRPYS PTAEGPGSAA AMTEGYGSDV VTLASSIATQ PELITVHMEK
GDKGFGFTIA DCGSGSSGGQ KVKQIVDYPR CRGLKEGDIL VEVNKRNVQS MSHNQVVDLL
SKCPRGSEVT MLVQRGEGTV CVWLSGCQLE RKDSQGSSQH SVCSHRSTHT DSPARAVLPP
LEPPTNGTLQ KKPDPFKIWA QSRSMYESRM PDSQEQDIFL WRKDTGFGFR ILGGNEPGEP
IYIGHIVKYG AADEDGRLRS GDELICVDGT AVVGKSHQLV VQLMQQAAKQ GHVNLTVRRK
TGYGVCKGEG DVPPSPASSH HSSTQAPSLT EEKRTPQGSQ NSLNTVSSGS GSTSGIGSGG
GGGSGSAVVA VAPAALQPYD VEIQRGENEG FGFVIVSSVS RPDAGTTFAG NACVAMPHKI
GRIIEGSPAD RCGKLKVGDR ILAVNGCSIT NKSHSDIVNL IKEAGNTVTL RIIPGDESSN
ASLLTNAEKI ATITTTHTPQ SSSEPRDSKG FGFSLRGGKE YNMDLYVLRL AEDGAAVRNG
KMRVGDEILE INGESTKNMK HSRAIELIKN GGRRARLVLK RGDGSVPEYD GPNDGYPAPP
GPQNLSEMRS LPSNGRFHLS SESSYTSEYH PPPWPQEHRL RERERERDQG REEYKDYAHY
PKAPHHLHHH HTWNNSNHSG PRAHSPSPSP ENDKKNSRRK VKKSESESGI AKLFKTLRKE
GGFGKKSSDR DLRGRGYERS PERGSQSRPQ TRRGSLDRSP SHKRNSSPDR RRAKSVDRRT
DRWQRDYSPD SRASSQVLLQ QAATPDRHLR PQREAHTPGR NYLREEGYLT STPERSNNAQ
AVLLARSHTP ERGLKNGNVL RDVSPSSRGD SISNGTPERR YRRESDSSSS SSYLEEAATP
RLKDYYNALK ANGANGTNAG RAPTQHPQSK RRLYKENHTD LSI
//
