GenomeNet

Database: UniProt
Entry: A0A150G4H1_GONPE
LinkDB: A0A150G4H1_GONPE
Original site: A0A150G4H1_GONPE 
ID   A0A150G4H1_GONPE        Unreviewed;       506 AA.
AC   A0A150G4H1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=PDZ domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GPECTOR_63g44 {ECO:0000313|EMBL:KXZ44718.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ44718.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50A family.
CC       {ECO:0000256|ARBA:ARBA00009989}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXZ44718.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LSYV01000064; KXZ44718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150G4H1; -.
DR   STRING; 33097.A0A150G4H1; -.
DR   OrthoDB; 3675515at2759; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        78..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        449..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        480..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..492
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   DOMAIN          272..324
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|Pfam:PF17820"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  50708 MW;  0F90185D02ABEA21 CRC64;
     MVDLPSAPPL RDGECRPRAD DVVREPHQRS VGLEASTSEL EQRSGFLGLG DLLQPKSAIL
     LGGLFSAVGY DTSKPSSVLA AIGVLAVIVA VHEAGHFAAA RLQGIRVTRF AVGFGPTLVK
     YQDGEVEYCL NAIPLGGYVA FPEDDPAASN PSKAATDAPA ADGAASASSP STSGAEGAAA
     ASSPAATTTA TAATSTSATA AAPATPSYSP DDPDLLKNRP IAQRALVISA GVIANIVFAY
     LILLLQISTV GKAETAFLPG VRVALPEAPA AVAASAGARG GLVSGDVLLR IGDVTVPAAP
     SQVGESVAAI RAAAGKPLEL TVRRAGTEAA ADGAASGSGQ VLKLRVTPEA GADGQGRLGV
     QLSSNTYIKH TYAANAGEVL AMTQSEFNRL AGTVFGGLQQ IITNFGAMSG QLSGPVAIVA
     AGSEVVRTDA AGLFQFAAIV NINLAAVNIL PLPALDGGYL ALLALEALRG GRKLPAGLEG
     GIMASGFLVL TALGMGLVIR DTLNLL
//
DBGET integrated database retrieval system