SIPL2_ORYSJ
ID SIPL2_ORYSJ Reviewed; 534 AA.
AC Q53P98; Q0IT05; Q53NS0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Signal peptide peptidase-like 2;
DE Short=OsSPPL2;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=SPPL2; OrderedLocusNames=Os11g0433200, LOC_Os11g24540;
GN ORFNames=OsJ_33780;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-534.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19688213; DOI=10.1007/s00299-009-0760-9;
RA Tamura T., Kuroda M., Oikawa T., Kyozuka J., Terauchi K., Ishimaru Y.,
RA Abe K., Asakura T.;
RT "Signal peptide peptidases are expressed in the shoot apex of rice,
RT localized to the endoplasmic reticulum.";
RL Plant Cell Rep. 28:1615-1621(2009).
CC -!- FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that
CC cleaves type II membrane signal peptides in the hydrophobic plane of
CC the membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX96394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF28160.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC128642; AAX92993.1; -; Genomic_DNA.
DR EMBL; AC133931; AAX96394.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000010; ABA93124.1; -; Genomic_DNA.
DR EMBL; DP000010; ABG22469.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF28160.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000148; EEE52048.1; -; Genomic_DNA.
DR EMBL; AK100614; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015617346.1; XM_015761860.1.
DR AlphaFoldDB; Q53P98; -.
DR STRING; 4530.OS11T0433200-02; -.
DR PaxDb; Q53P98; -.
DR GeneID; 4350402; -.
DR KEGG; osa:4350402; -.
DR eggNOG; KOG2442; Eukaryota.
DR HOGENOM; CLU_023799_4_1_1; -.
DR InParanoid; Q53P98; -.
DR OrthoDB; 535101at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR Genevisible; Q53P98; OS.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; IBA:GO_Central.
DR GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IBA:GO_Central.
DR GO; GO:0033619; P:membrane protein proteolysis; IBA:GO_Central.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007369; Peptidase_A22B_SPP.
DR InterPro; IPR006639; Preselin/SPP.
DR PANTHER; PTHR12174; PTHR12174; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04258; Peptidase_A22B; 1.
DR SMART; SM00730; PSN; 1.
PE 2: Evidence at transcript level;
KW Endosome; Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..534
FT /note="Signal peptide peptidase-like 2"
FT /id="PRO_0000419101"
FT TOPO_DOM 28..198
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..276
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..428
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..491
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 93..172
FT /note="PA"
FT MOTIF 493..495
FT /note="PAL"
FT ACT_SITE 387
FT /evidence="ECO:0000250"
FT ACT_SITE 439
FT /evidence="ECO:0000250"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 534 AA; 58622 MW; 082E0798D2063A52 CRC64;
MATHHARRLP AAAAVLLLVL LAGGSAADDA SSDDDAGVPP SPGCSNKFQL VKVKNWVNGT
EGTIVVGLSA RFGASVPRDI HEAQKTFAVL ANPLDCCSNS TSKLTNYIAI AQRGECAFTA
KAKIAQTGGA VGLLVINDNE ELYKMVCSDN DTSINVTIPV VMIPQSAGKK MKGLLDQGAR
LEVQLYSPNR PVVDLSACFL WIMAIGTIVC ASLWTEFVAC EQVDERYNQL TRKDGPNSGT
TNREDKEIFE ISAKGAIVFI LVASVFLLLL FYFMSSWFVW LLIVLFCIGG IEGMHVCLVT
LLTRICKDCG QKTVQLPFFG EVLTLSVLIV PFCTIFAILW AVYRHASFAW IGQDILGICL
MITVLQMARL PNIRVASALL SAAFVYDVFW VFISPLIFHE SVMIAVARGD NSGEAIPMLL
RIPRFFDPWG GYDMIGFGDI IFPGLLVAFS YRFDRASKRG LFNGYFLWLT VGYAVGLFLT
YLALFLMDGH GQPALLYLVP CTLGLIVILG WFRGELHDLW NYGRSQTENL VDEP
