ID A0A2Y9NGD0_DELLE Unreviewed; 1257 AA.
AC A0A2Y9NGD0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 isoform X17 {ECO:0000313|RefSeq:XP_022428334.1, ECO:0000313|RefSeq:XP_022428335.1};
GN Name=MAGI1 {ECO:0000313|RefSeq:XP_022428334.1,
GN ECO:0000313|RefSeq:XP_022428335.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022428334.1};
RN [1] {ECO:0000313|RefSeq:XP_022428334.1, ECO:0000313|RefSeq:XP_022428335.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022428334.1,
RC ECO:0000313|RefSeq:XP_022428335.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_022428334.1; XM_022572626.1.
DR RefSeq; XP_022428335.1; XM_022572627.2.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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; PF16663; MAGI_u1; 1.
DR Pfam; PF16666; MAGI_u5; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00228; PDZ; 5.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 5.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50106; PDZ; 5.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|RefSeq:XP_022428334.1,
KW ECO:0000313|RefSeq:XP_022428335.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transferase {ECO:0000313|RefSeq:XP_022428334.1,
KW ECO:0000313|RefSeq:XP_022428335.1}.
FT DOMAIN 73..106
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 133..166
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 234..303
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 405..483
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 603..685
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 765..861
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 920..1002
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 138367 MW; 3D25C86E27F51F3A CRC64;
MQNAGIVHVE NEEDDDVPEM NSSFTADSGD QEEHSLQEAT LPPVNSSIIA APITDPSQKF
PQYLPLSAED NLGPLPENWE MAYTENGEVY FIDHNTKTTS WLDPRCLNKQ QKPLEECEDD
EEGIHTEELD SELELPAGWE KIDDPVYGIY YVDHINRKTQ YENPVLEAKR KKQLEQQQQQ
QQQPEEWTED HSSLVPPIIP NHPPSNPEQA REAPLQGKPF FTRNPSELKG KFIHTKLRKS
SRGFGFTVVG GDEPDEFLQI KSLVLDGPAA LDGKMETGDV IVSVNDTCVL GHTHAQVVKI
FQSIPIGASV DLELCRGYPL PFDPDDPNTS LVTSVAILDK EPIIVNGQET YDSPASHSSK
TGKANGMKDA RPSSPADVAS NGSHGYPNDT VSLASSIATQ PELITVHIVK GPMGFGFTIA
DSPGGGGQRV KQIVDSPRCR GLKEGDLIVE VNKKNVQALT HNQVVDMLIE CPKGSEVTLL
VQRGGLPVPK KSPKSQPLER KDSQNSSQHS AASHRSLHTA SPGHGTQVLP EFPPAEAPAP
DQTDSSGQKK PDPFKIWAQS RSMYENRPMS PSPASGLSKG ERDKEINSTN FGECQIPDYQ
EQDIFLWRKE TGFGFRILGG NEPGEPIYIG HIVPLGAADT DGRLRSGDEL ICVDGTPVIG
KSHQLVVQLM QQAAKQGHVN LTVRRKVVFA ASKTENEVPS PASSHHSSNQ PASLTEEKRT
PQGSQNSLNT VSSGSGSTSG IGSGGGGGSG VVSTGVVSTV VQPYDVEIRR GENEGFGFVI
VSSVSRPEAG TTFAGNACVA MPHKIGRIIE GSPADRCGKL KVGDRILAVN GCSITNKSHS
DIVNLIKEAG NTVTLRIIPG DESSNATLLT NAEKIATITT THTPSQQGAQ ETSRNTTKPK
PESQFEFKAP QGTQEQDFYT VELERGAKGF GFSLRGGREY NMDLYVLRLA EDGPAERCGK
MRVGDEILEI NGETTKNMKH SRAIELIKNG GRRVRLFLKR GDGSVPEYDP SSDGNGPPTG
PQGVPEMRAA PPDRRQHPSL ESSYPPDLHK SSPHGEKRAH VRDPKGCREY SRQPNEHHTW
NGTSRKPDSG ACRPKDRAPE GRRDAQPERM VTNGPKRRPP EKRREGTRSA DNTLERREKQ
EKREASPERR RERSPTRRRD GSPGRRRRSL ERLLDQRSPE RKRGSSPERR AKSTDRRRTR
SPERRRERSL EKRSKEDKGG HRERDETSLK QDAGRSSRHP PEQRRRPYKE CSTDLSI
//
