ID A0A337SIQ5_FELCA Unreviewed; 1452 AA.
AC A0A337SIQ5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 2 {ECO:0000313|Ensembl:ENSFCAP00000046947.1};
GN Name=MAGI2 {ECO:0000313|Ensembl:ENSFCAP00000046947.1,
GN ECO:0000313|VGNC:VGNC:80620};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000046947.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000046947.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000046947.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000046947.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000046947.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000046947.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000046947.1};
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 EMBL; AANG04003224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000046947; -.
DR Ensembl; ENSFCAT00000052234.2; ENSFCAP00000046947.1; ENSFCAG00000030754.4.
DR VGNC; VGNC:80620; MAGI2.
DR GeneTree; ENSGT00940000155057; -.
DR InParanoid; A0A337SIQ5; -.
DR OMA; XYRSEVK; -.
DR Proteomes; UP000011712; Chromosome A2.
DR Bgee; ENSFCAG00000030754; Expressed in brain and 9 other cell types or tissues.
DR GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; IBA:GO_Central.
DR GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR GO; GO:0070699; F:type II activin receptor binding; IBA:GO_Central.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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:SF27; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF00595; PDZ; 6.
DR Pfam; PF00397; WW; 1.
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:UP000011712};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 17..101
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 109..185
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 301..334
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 347..380
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 425..494
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 604..667
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 777..859
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 919..1009
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1140..1222
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 205..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1452 AA; 158449 MW; FB4A3F39ABECA912 CRC64;
MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL
VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS
VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED
NYYGTPKPPA EPAPLLLNVT DQILPGATPS AEGKRKRNKS VSNMEKASIE PPEEEEEERP
VVNGNGVVTP ESSEHEDKSA GASGETPSQP YPAPVYSQPE ELKEQMDDAK PTKPEENEES
DPLPDNWEMA YTEKGEVYFI DHNTKTTSWL DPRLAKKAKP PEECKENELP YGWEKIDDPI
YGTYYVDHIN RRTQFENPVL EAKRKLQQHN MPHTELGTKP LQAPGFREKP LFTRDASQLK
GTFLSTTLKK SNMGFGFTII GGDEPDEFLQ VKSVIPDGPA AQDGKMETGD VIVYINEVCV
LGHTHADVVK LFQSVPIGQS VNLVLCRGYP LPFDPEDPAN SMVPPLAIME RPPPVMVNGR
HNYETYLEYI SRTSQSVPDI TDRPPHSLHS MPADGQLDGT YPPPVHDDNV SMASSGATQA
ELMTLTIVKG AQGFGFTIAD SPTGQRVKQI LDIQGCPGLC EGDLIVEINQ QNVQNLSHTE
VVDILKDCPI GSETSLIIHR GGFFSPWKTP KPIMDRWENQ GSPQTSLSAP AIPQNLPFPP
ALHRTSFPDS TEAFDPRKPD PYELYEKSRA IYESRQQVPP RTSFRMDSSG PDYKELDVHL
RRMESGFGFR ILGGDEPGQP ILIGAVIAMG SADRDGRLHP GDELVYVDGI PVAGKTHRYV
IDLMHHAARN GQVNLTVRRK VLCGGEPCPE NGRSPGSVST HHSSPRSDYA AYTNSNHAAP
SSNASPPEGF ASHSLQTSDV VIHRKENEGF GFVIISSLNR PESGSTITVP HKIGRIIDGS
PADRCAKLKV GDRILAVNGQ SIINMPHADI VKLIKDAGLS VTLRIIPQEE LSSPASAPSS
EKQSPMAQQS PLAQPSPATP NSPVAQPAPP QPLQLQGHEN SYRSEVKARQ DVKPDIRQPP
FTDYRQPPLD YRQPPGGDYQ QPPPLDYRQP PLLDYRQHSP DTRQYPLADY RQPQDFDYFT
VDMEKGAKGF GFSIRGGREY KMDLYVLRLA EDGPAIRNGR MRVGDQIIEI NGESTRDMTH
ARAIELIKSG GRRVRLLLKR GTGQVPEYDE PNCWSSPAAA SPGLPEVGVS LEDVLSPFSP
SHPAPPSDPS HQIGPDPTWD IKREHDVRKP KELSAGGQKK QRLGEQRERS ASPQRAARPR
LEEAPGGQGR PEAGRPSSEA RAPGPAAADA ADAARAGGKE GPRAAVGPEL GRREGPGAAP
AFAGPGRGGG AERPGAREAE GRAGARAGPR QGARPPGGAP ARKAAVAPGP WKVPGSDKLP
GVLKPGASAA GR
//
