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Database: UniProt
Entry: A0A3Q7R686_VULVU
LinkDB: A0A3Q7R686_VULVU
Original site: A0A3Q7R686_VULVU 
ID   A0A3Q7R686_VULVU        Unreviewed;      1484 AA.
AC   A0A3Q7R686;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 isoform X7 {ECO:0000313|RefSeq:XP_025840882.1};
GN   Name=MAGI1 {ECO:0000313|RefSeq:XP_025840882.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025840882.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025840882.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025840882.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025840882.1};
RG   RefSeq;
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   RefSeq; XP_025840882.1; XM_025985097.1.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; -; 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; 5.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 6.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
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   Kinase {ECO:0000313|RefSeq:XP_025840882.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|RefSeq:XP_025840882.1}.
FT   DOMAIN          17..104
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          95..188
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   DOMAIN          299..332
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          346..379
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          463..532
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          634..712
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          832..914
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          989..1084
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1142..1224
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          235..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1224..1484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..973
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1275..1450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1484 AA;  162952 MW;  342730EF09F1A2F8 CRC64;
     MSRVIQKKNH WTSKIHECTV RRGPQGELGV TVLGGAENGE FPYVGAVAEA PKGLPGGGEG
     PRLGEGELLL EVQGIRVSGL PRYDVLGVID SCKEAVTFKA VRQGGKLNKD LRHFLNQRFQ
     KGSPDHELQQ TIRDNLYRHA VPCTTRSPRE GEVPGVDYNF LTVKEFLDLE QSGTLLEVGT
     YEGNYYGTPK PPSQPVSGKV ITTDALQSLQ SGSKQSTPKR TKSYNDMQNA GIVHAENEEE
     DDVPEMNSSF TADSGDQEEH TLQEAALPPV NSSIVAAPIT DASQKFPQYL PLCAEDNLGP
     LPENWEMAYT ENGEVYFIDH NTKTTSWLDP RCLNKQQKPL EECEDDELPA GWEKIEDPVY
     GIYYVDHINR KTQYENPVLE AKRKKQLEQQ QQPQQQQQQQ QQQQQQQQQQ QPPEEWTEDH
     SSLVPPVIPN HPPSNPEPAR EAPLQGKPFF TRNPSELKGK FIHTKLRKSS RGFGFTVVGG
     DEPDEFLQIK SLVLDGPAAL DGKMETGDVI VSVNDTCVLG HTHAQVVKIF QSIPIGASVD
     LELCRGYPLP FDPDDPNTSL VTSVAILDKE PIIVNGQETY DSPASHSSKT GKVNGMKDAR
     PSSPADVASN GSHGYPNDTV SLASSIATQP ELITVHIVKG PMGFGFTIAD SPGGGGQRVK
     QIVDSPRCRG LKEGDLIVEV NKKNVQALTH NQVVDMLIEC PKGSEVTLLV QRGGLPVPKK
     SPKSQPLERK DSQNSSQHSV SSHRSLHTAS PSHSTQVLPE YPPAEAPAPD QTDSSGQKKP
     DPFKIWAQSR SMYENRPMSP SPASGLSKGE REREINSTSF GECQIPDCQE QDIFLWRKET
     GFGFRILGGN EPGEPIYIGH IVPLGAADTD GRLRSGDELI CVDGTPVIGK SHQLVVQLMQ
     QAAKQGHVNL TVRRKVVFAA PKAENEVPSP ASSHHSSNQP ASLTEEKRTP QGSQNSLNTV
     SSGSGSTSGI GSGGGGGSGV VSTAVQPYDV EIRRGENEGF GFVIVSSVSR PEAGTTFGNA
     CVAMPHKIGR IIEGSPADRC GKLKVGDRIL AVNGCSITNK SHSDIVNLIK EAGNTVTLRI
     IPGDESSNAT LLTNAEKIAT ITTTHTPSQQ GTQETRNTTK PKPESQFEFK APQAAQEQDF
     YTVELERGAK GFGFSLRGGR EYNMDLYVLR LAEDGPAERC GKMRIGDEIL EINGETTKNM
     KHSRAIELIK NGGRRVRLFL KRGDGSVPEY DPSSDRHGPA AAAGPQGVPE VRAAPPDRRP
     HPSLESSYPP DLHQSSQHGE KRAHGRDPKG SSRESSRQPN EHHTWNGTSR RPDGGACRPK
     DRAPEGRREA PPERLVPNGP KRRSPEKQRR EGTRSADTTL ERRERPERRR ERSPGRRRDG
     SPGARRRSLE RLLEQTRPAE RRRGSSPERR AKSTERRRAR SPERRRERSL EKRDRDRDRD
     REEQRGGARG RAEPGPKPAP SGCRPAAPEP RRRPYKECST DLSI
//
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