ID A0A2Y9N2B7_DELLE Unreviewed; 1442 AA.
AC A0A2Y9N2B7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 isoform X24 {ECO:0000313|RefSeq:XP_022428345.1};
GN Name=MAGI1 {ECO:0000313|RefSeq:XP_022428345.1};
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_022428345.1};
RN [1] {ECO:0000313|RefSeq:XP_022428345.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022428345.1};
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_022428345.1; XM_022572637.1.
DR Proteomes; UP000248483; 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; 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_022428345.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|RefSeq:XP_022428345.1}.
FT DOMAIN 17..105
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 96..189
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 300..333
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 347..380
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 448..517
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 619..697
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 789..871
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 951..1046
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1105..1187
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 237..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1442 AA; 158607 MW; FBCF607904DDDF96 CRC64;
MSKVIQKKNH WTSRVHEFTV KRGPQGELGV TVLGGAENGE FPYVGAVAAA EAAGLPGGGQ
GPRLGEGELL LEVQGIRVSG LPRYDILGVI DSCKEAVTFK AVRQGGKLNK DLRHFLNQRF
QKGSPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYN FLTVKEFLDL EQSGTLLEVG
TYEGNYYGTP KPPSQPLSGK VITTDALQSL HSGSKQSTPK RTKSYNDMQN AGIVHVENEE
DDDVPEMNSS FTADSGDQEE HSLQEATLPP VNSSIIAAPI TDPSQKFPQY LPLSAEDNLG
PLPENWEMAY TENGEVYFID HNTKTTSWLD PRCLNKQQKP LEECEDDELP AGWEKIDDPV
YGIYYVDHIN RKTQYENPVL EAKRKKQLEQ QQQQQQQPEE WTEDHSSLVP PIIPNHPPSN
PEQAREAPLQ GKPFFTRNPS ELKGKFIHTK LRKSSRGFGF TVVGGDEPDE FLQIKSLVLD
GPAALDGKME TGDVIVSVND TCVLGHTHAQ VVKIFQSIPI GASVDLELCR GYPLPFDPDD
PNTSLVTSVA ILDKEPIIVN GQETYDSPAS HSSKTGKANG MKDARPSSPA DVASNGSHGY
PNDTVSLASS IATQPELITV HIVKGPMGFG FTIADSPGGG GQRVKQIVDS PRCRGLKEGD
LIVEVNKKNV QALTHNQVVD MLIECPKGSE VTLLVQRGGL PVPKKSPKSQ PLERKDSQNS
SQHSAASHRS LHTASPGHGT QVLPEFPPAE APAPDQTDSS GQKKPDPFKI WAQSRSMYEN
RLPDYQEQDI FLWRKETGFG FRILGGNEPG EPIYIGHIVP LGAADTDGRL RSGDELICVD
GTPVIGKSHQ LVVQLMQQAA KQGHVNLTVR RKVVFAASKT ENEVPSPASS HHSSNQPASL
TEEKRTPQGS QNSLNTVSSG SGSTSGIGSG GGGGSGVVST GVVSTVVQPY DVEIRRGENE
GFGFVIVSSV SRPEAGTTFG NACVAMPHKI GRIIEGSPAD RCGKLKVGDR ILAVNGCSIT
NKSHSDIVNL IKEAGNTVTL RIIPGDESSN ATLLTNAEKI ATITTTHTPS QQGAQETSRN
TTKPKPESQF EFKAPQGTQE QDFYTVELER GAKGFGFSLR GGREYNMDLY VLRLAEDGPA
ERCGKMRVGD EILEINGETT KNMKHSRAIE LIKNGGRRVR LFLKRGDGSV PEYDPSSDGN
GPPTGPQGVP EMRAAPPDRR QHPSLESSYP PDLHKSSPHG EKRAHVRDPK GCREYSRQPN
EHHTWNGTSR KPDSGACRPK DRAPEGRRDA QPERMVTNGP KRRPPEKRRE GTRSADNTLE
RREKQEKREA SPERRRERSP TRRRDGSPGR RRRSLERLLD QRSPERKRGS SPERRAKSTD
RRRTRSPERR RERSLEKRSK EDKGGHRERD ETSLKQDAGR SSRHPPEQRR RPYKECSTDL
SI
//
