BST1_USTMA
ID BST1_USTMA Reviewed; 1520 AA.
AC Q4P782; A0A0D1C2I5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=BST1; ORFNames=UMAG_04031;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
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DR EMBL; CM003150; KIS67987.1; -; Genomic_DNA.
DR RefSeq; XP_011390476.1; XM_011392174.1.
DR AlphaFoldDB; Q4P782; -.
DR STRING; 5270.UM04031P0; -.
DR ESTHER; ustma-q4p782; PGAP1.
DR EnsemblFungi; KIS67987; KIS67987; UMAG_04031.
DR GeneID; 23564323; -.
DR KEGG; uma:UMAG_04031; -.
DR VEuPathDB; FungiDB:UMAG_04031; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_251631_0_0_1; -.
DR InParanoid; Q4P782; -.
DR OMA; QWELIPP; -.
DR OrthoDB; 438490at2759; -.
DR Proteomes; UP000000561; Chromosome 11.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050185; F:phosphatidylinositol deacylase activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495; PTHR15495; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1520
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277643"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 886..908
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 915..937
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1018..1038
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1052..1072
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1087..1107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 201
FT /evidence="ECO:0000250"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1520 AA; 167119 MW; A9F9675E691B2766 CRC64;
MTTTSRSGRQ LWLPWLILVV SLTLITYSVD SFIRLPQQLG VSQQCRMSRM WPAYIDHTSN
LEPFSPSGLW RKYRLYLYRE RHFEPMDLPT GSPALFVPGN SGSYGQVRSV ASSASRQFYK
ENGSGARRDE WKDAPPGVAH TDWYTIDFNE DFSAFSGTTL IEQATFINEV VSYLSDRYAS
AATHSYAAGE RNTTVPILAH SMGGIAARLT AHLPNYPVGN IDTIVTLSTP HAFPPVPFDS
SVEYVYSLIN TPLDASRVTS RSARNVPPLL VSIAGGLLDT QLPSDPSSLS LARIGEAIAP
SRISTYTGSL PSLWSSVDHV AVMWCDQLRE KIARGFLLDM MAFGRVSDER NAGGVSGRSS
VLRRRRELWR RALSLFDVSD AGNGEIGPLE LTPSPDWLLE EDRETFVVEN ESPSFQRPTS
GPDSALSVDQ QNTVFRIPAR MGDSDDGLHA FELITNLCVG WNPSSGMGAP LPQPVELVVQ
LCTSNPDSSD PVSGQRTSCR LVMPWQWELI PPSFLPRTDI LMQESSQHID THLPENRPFP
SADEIYHVPG YAFQRLRLDA DLLQRQRIDW IRVERKTDSG VFVHQRGLKS FVRGGWMRQA
AGRLKKHGSS LLLTQDQDSD IQHHYQDAGF ATTSAIPIAS EWLLKGFSSS LLARRIELVP
SQCLVENLAL YTLQSNDESL HSTDASFSPF MRVSDRATGD SRWYPQLASP ELVRRIRART
YKGEPITFPL SLHGNAPFMP PARDSLNEIR VQLWTDQALL RPVPGKSLPC RSSVDSIRLS
VDWKASAGLV LLRYRFLLAA WPLGLLSVCI GLSWLTWTQK PELPFPSPLT SITQPVFRTP
FIGNRVDPLL GLLACTAIAL ILLDGMRLWL YRCMSSAEAR GPTSSLIGMV LGLHNHASSA
GLIPCFLLVS YATLLVIVAI IQWSFSLIAA IVTRFGLAHK LDWVGAATAS SDPLKWNRRS
MAGLAILLLS VVLLVPHQFV FLIMFLLQLL NTLRALLELQ SNRGPPQSQE SRFHQHLSIL
MMLVLLLPQK ASFLVTWVRN LASVGIKTPN TMAAWMDHNL LDVAPIVVLV WLMAGGRMLE
PARSKMEAKA IVFGFSIVGW YALVWGIRYT YRTYDAFNAL CLVLAVCHWR SRRAGSRSHY
SQGHAACNVA KHSDETSGML HAHGKDEGVN LGDAPAEEFE LRSGLASARL PIHHLALPSS
VDPQSGGASI AEGNASTCAV VESSAQTNLG GDKLDELIAD YLDVLDRYQR ARNATSALFS
SGYLKLTRAK IELGASRLSS NSYDSRLLAE VRATISNESS SQSSCGGLPA QASEISHISV
ARVQPDYSHL ENDDYVLIQD MDESKVEKAD STIAGLRRRA AVGVTLSETD VVEGSGPHKH
SPRGSLNDSV LRPVRVSAAD AEGRGDAIKM SAVQPEKGHS KNSKYDVIST NQGDDQLGRM
EQTKKVAAKP DALLQFGGLP STALRGAQVD LRKALNQLLG AESHVHDDGV LQLALRLEVL
TSAISTLKAT AANQSECEKR
