ID I3KKZ0_ORENI Unreviewed; 1448 AA.
AC I3KKZ0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 1a {ECO:0000313|Ensembl:ENSONIP00000021785.2};
GN Name=MAGI1 {ECO:0000313|Ensembl:ENSONIP00000021785.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000021785.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000021785.2}
RP IDENTIFICATION.
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 STRING; 8128.ENSONIP00000063122; -.
DR Ensembl; ENSONIT00000021804.2; ENSONIP00000021785.2; ENSONIG00000017273.2.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00940000155820; -.
DR HOGENOM; CLU_004562_1_0_1; -.
DR TreeFam; TF316816; -.
DR Proteomes; UP000005207; Linkage group LG20.
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: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; 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:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 17..100
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 108..184
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 294..327
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 341..374
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 426..495
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 595..673
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 798..880
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 959..1055
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1086..1168
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 200..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1448 AA; 159238 MW; DE8761502C127C75 CRC64;
MSKVIQRKNH WITKVNECTV IRDAYGELNV ELRGGAENGE FPYIGQVKED AVLYQDGKLS
EGELLLEVER VSVSGLPLYD IFTVIGCCKG PVRLKTVRQG HKLNKDLKHY LSLRFQKSSP
DHELQKTIRA NLYRHAVPCT TRPPRDGEVP GVDYNFLSVE EFLELEESGT LLEIGTYEGN
YYGTPKPPRQ PIIGTVILSD AGSHQSTPTR TKSYNDMQNA RVVPADDDDD DQATEMNNSF
TGEGTDESRS GILRPYPARD SALSCGLNNA ATSTAESGQQ TLAEPQVSPE DPLGPLPENW
EMAYTENGEL YFIDHNTKTT SWLDPRCRDR TSRPLEECDD DELPPGWERI DDPVYGVYYV
DHINRKTQYE NPVVEARRRK ILEQQQQPQP PEEWIEEHSS LFLAHSAGGK PFFTRNPAEL
KGTFINTKLK KSCRGFGFTV VGGDEPDEFL QIKSLVLDGP AALDGKMETG DVIVSVNDTI
VLGYTHAQVV KIFQSIPIGS MVDLSLCRGY PLPFDPDDPN TSLVTSVAIL DKEPIIVNGQ
ETFDPPSNQA GPINGLREPR PHSPSAEVAS NGSHGYTSDV VTLASSIATQ PELITIHMEK
GDKGFGFTIA DSLTGGGQRV KQIVDYPRCR GLKEGDILME VNKRNVQNMS HNQVVDLLSK
CPRGSEVTML VQRGMYYKSY KCISTGLERK DSQSSSQHSV CSHRSTHTDS PSHPPSVMPS
EAVVPTPAAP TQPLPGLPPQ DPADGTLTLQ KKPDPFKIWA QSRSMYESRP DPVTKGASER
EVPHCFSCVS VPDCQEQDIF LWRKDTGFGF RILGGNEPGE PIYIGHIVKY GAADEDGRLR
SGDELICVDG TAVVGKSHQL VVQLMQQAAK QGHVNLTVRR KSPGYGVSKG EGDVPPSPAS
SHHSSTQAPS LTEGKRTPQG SQNSLNTVSS GSGSTSGIGS GGGGGSGSAV VPASLQPYDV
EIQRGENEGF GFVIVSSVSR PDAGTTFAGN ACVAMPHKIG RIIEGSPADR CGKLKVGDRI
LAVNGCSITN KSHSDIVNLI KEAGNTVSLR IIPGDESSNA SLLTNAEKIA TITTTHTPQS
DAEFYSVDLE RDSKGFGFSL RGGREYNMDL YVLRLAEDGA AVRNGKMRVG DEILEINGES
TKNMKHSRAI ELIKNGGRRA RLVLKRGDGS VPEYDGSNDG HPSAPGAQNT PEVRTLPPKS
RYHTSLESSY PPELHKPSRQ EEAVRGRDMD RNRDRAGSNQ MDYQDWQFKP HHHHTWNNNH
SQSSPRQQSP DNSNSSSNGN KKSWGRKVKK SESESGISKL LKTLRKDNSG KKAAAAEKLR
ERELSNSSST LDGRFRPQRR GSLDRSPTRK RASSPDHRRA KSMDRRAERA HRDRTPERDY
DDGGFLAVTP DRKYNERRRK KTVCTDAMGR SSTRFQLQAT VFSVVEKCNF TLHESALCHN
TSRSCHEI
//
