ID A0A2U9BEE1_SCOMX Unreviewed; 1487 AA.
AC A0A2U9BEE1;
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=Putative membrane-associated guanylate kinase WW and PDZ domain-containing protein 3-like {ECO:0000313|EMBL:AWP02408.1};
GN ORFNames=SMAX5B_005556 {ECO:0000313|EMBL:AWP02408.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP02408.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP02408.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; CP026248; AWP02408.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000011918; -.
DR Proteomes; UP000246464; Chromosome 6.
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; cd00987; PDZ_serine_protease; 1.
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:SF65; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 3 ISOFORM X1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 4.
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|EMBL:AWP02408.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Transferase {ECO:0000313|EMBL:AWP02408.1}.
FT DOMAIN 65..103
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 111..187
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 287..320
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 333..366
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 409..478
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 591..654
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 742..825
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 866..953
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1025..1107
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 217..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 161743 MW; F50906B95F433CA2 CRC64;
MSRTLKKKKH WSGKVVECAV SWGNLGDFGS VVEVLGGAEL GQFPHLGQMK LDVLVCHVGK
LPYYGDVLLE VNGTPVSGLT NRDTLAVIRH FREPVRLKTV KPGKVLNSDL RHYLSLQFQK
GSLDHKLQQI IRDNLYLRTI PCTTRLPRDG EVPGVDYNFI SVGDFRILEE SGLLLESGTY
DGNYYGTPKP PAEPNLVQPD LVDQVLFDED YVGDVPRKRT TSVSNMDRKD STVPEEEDDD
DRPPLVNGLP ELKERADWRK AVPSYTQSSS SMDFRTWSSL PRDDSLEPLP LNWEMAYTET
GMVYFIDHNT KTTTWLDPRL AKKAKPPEKC EDGELPYGWE EIDDPQYGTY YVDHINQKTQ
FENPVLEAKK KLSQETAAIQ QAAAAPSQGK GGAFGFTADP NQLNGELYHT ALKKSAQGFG
FTIIGGDRTD EFLQVKNVLG DGPAAHDNKM ASGDVIVEIN GMCVLGKTHP EVVQMFQSIP
INQYVDMVLC RGYPLPPDVD LTSDDPLPPP PPPANAQPQQ ALHGGEVVTA VPLINGQPLL
VKGDVLHGSS QELHYVTTDA SGRPVVAALP NGRQGERGEM ASAMLQPELV SVPLVKGPGG
FGFAIADCPL GQKVKMILDA QWCRGLQKGD VIKDINRQNV QTLSHAQVVD ILKDLPVGSE
VNVLVLRGGQ TSPVKSLKPR QDMTASTETL DGIADSAPQA LPYHSNTSTL RSADSPKRDA
TEMYLKSKAL LESRQPYTKD IDVFLKRDIE TGFGFRVLGG EGPQQPVYIG AIVASGAAEK
DGRLRAGDEL IGIDGVMVKG RSHKQVLDLM TNAARNGQVM LTVRRKVIYR DPTEEEALEM
APVLVNGSPK LPRLPMPSAL DHESFDITLH RKDTEGFGFV ILTSKSKPPL GVIPHKIGRI
IEGSPTDRCG LLHVGDRISA VNGRSIIELS HNDIVLLIKE AGNVVTLTVV PEDEYKGPPS
GASSAKQSPA LQHRAMGQRS ALQDDRYNLD LEERRDGVSW SDHNTLPLSE QGTLCVTGPN
QGCLTVELER GPRGFGFSLR GGTEYNMGLY ILRLAEDGAA QLDGRIHVGD EIVEINGEPA
RGISHTRAIE LIQAGGSKVA LLLRPGAGLA QDGSQRDQKL ISPSGYSREV FFSDTSPLSP
PFSPGASLFV SPPFAGKLKH SVSWSSISPR RLKPRGSSSG SSRGLSSVEE SGEWADKEAE
RLSPASPEHV KFYKRTRPAK DSSELSSPKK TLETFQAKEH HPSPRKTQSQ AQKETLSRSR
MPATRAETEY ASPRRSPQAG PPAAATPRGA ERQRGPRAAS KDTSGQESLS HEKKNGKGAS
LEIRRHAHGG EVEGRGERIR HGHEQDGFKR RVARESQHPR ASPHAARDGQ TGPGEDSGKR
DANGKGKPPE DRGRGREATN GKREPLLSFK EARARKVSVA SPAGAKGRQE AFPRGRESGS
KDAAVASVSC VPGTPQTPEG PLSPGPWKVP SSAKILSQAE VLRDPLR
//
