ID C1EF50_MICCC Unreviewed; 1120 AA.
AC C1EF50;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=MICPUN_103833 {ECO:0000313|EMBL:ACO66787.1};
OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO66787.1, ECO:0000313|Proteomes:UP000002009};
RN [1] {ECO:0000313|EMBL:ACO66787.1, ECO:0000313|Proteomes:UP000002009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins
CC which plays important roles in the quality control and ER-associated
CC degradation of GPI-anchored proteins. {ECO:0000256|RuleBase:RU365011}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|ARBA:ARBA00006931, ECO:0000256|RuleBase:RU365011}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; CP001331; ACO66787.1; -; Genomic_DNA.
DR RefSeq; XP_002505529.1; XM_002505483.1.
DR AlphaFoldDB; C1EF50; -.
DR STRING; 296587.C1EF50; -.
DR GeneID; 8248459; -.
DR KEGG; mis:MICPUN_103833; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG3724; Eukaryota.
DR InParanoid; C1EF50; -.
DR OrthoDB; 298238at2759; -.
DR Proteomes; UP000002009; Chromosome 13.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365011};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365011};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365011}.
FT TRANSMEM 243..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 310..331
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 808..829
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 873..897
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT DOMAIN 27..110
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 176..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 119120 MW; CD615AED23492FE8 CRC64;
MAYEHRPLSL EDARKTYLPS DDERAYWPKF TREHVATHAT LKDGWCVIHE RVYDITLFAI
THPGFHNAGQ VSTALAITRS LGKDATEEFE YVHSRLAWKQ LHDFQVGVIY RPDEDGPETP
VDARVDPPGH PIPHRGPARH PLPEWLGMER DFWQRYTGGV TEEVLDYLDE QGYPQERGGV
EEVSGGRWTK GGDGVGKREE TRSSVAEVMV AASGDEKEQM REARAAHRAR WRRERDERGK
RRMSRVGGAA AAVAAVALLA LGTRRRTKSA KLHTVAESGH PRSSMTETEE PSRPRRPQRP
PPRPSKPEPI PTVILVPLLL ALLSPLALAW ARALSAEFGG GPNRCAMTYM SPAYFPVPVN
ASSTTYALWL YRERAASTLT AGGAMASVGN GGGTGCGSAI WRPGRSIPGI FVPGNAGSYR
QVRSLASETA RRVDARRAAS GDAPDPEGTE TREEHVGVDW FTLDFNEELS AFHGAVALRQ
TEFAAFAIER VLARYPHGTP VIIAGHSMGG VVARAALLEL NRATTRRTAV DATVVTIATP
HEKSPAATQP AVARFYERTN RAWADERNVD VTSRVAIVSV GGGDADRQVR PARAKPPTAW
TNGMIGNRRK RFNVTHAVAG SIPGSTGVSA DHRCVVWCQQ IVVPIAETLL DVASDQRPDD
AVGRVALART RLGPTDEENQ KNQTPQKPKP KGTARLDAAA ALALDRFPSL VPIMLALAID
ALVVPQTTRR GGFGVEGQTV RGAVSLFAAP VFVRSRVVLV FLLGGFIGGG MDPWGGTHDG
VRGWAPLGVL RGVLSGVLSV PANLASAFAA YAFAAAALTL EALALDAVVR LSAKIYVKYV
RGPSHGRRRT TRRKDGDVTT VVDVSRRGFH VPFIATVTAT FVSIWCPGAG VAVALLARLA
SAVRTASVGL GPHPIAPVID DFGEGDAART CATLRLLLTC QSASMLAPSF VATVHALINS
SSGGEWTRLA SFVPVARAGW EDVVLAVCTA APAAFFAFAP SAYATLEVDW TSFNELPPAP
GTAVSAAASS RAVRPGDLAT LTGYVAAEAI ALRAAAPGCA HWAQHAAAAV TVLPLLAGSA
ATAWSARGVF SGGAHSRGGA DDGRDGGSTG ARGSGKPKAE
//
