SIP2_ORYSJ
ID SIP2_ORYSJ Reviewed; 343 AA.
AC B9FJ61; Q6I5K5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Signal peptide peptidase 2;
DE Short=OsSPP2;
DE EC=3.4.23.-;
DE AltName: Full=Intramembrane protease 2;
DE Short=IMP;
DE Short=IMPAS;
GN Name=SPP2; OrderedLocusNames=Os05g0436400, LOC_Os05g36070;
GN ORFNames=OJ1058_F05.2, OsJ_18668, OSJNBb0088F07.14;
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 [MRNA], GENE FAMILY, NOMENCLATURE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Nipponbare;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
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 [4]
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 [5]
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 [6]
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).
CC -!- FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that
CC cleaves type II membrane signal peptides in the hydrophobic plane of
CC the membrane. Catalyzes intramembrane proteolysis of some signal
CC peptides after they have been cleaved from a preprotein, resulting in
CC the release of the fragment from the ER membrane into the cytoplasm.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19688213}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19688213}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19688213}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in vegetative shoot apex, young
CC panicle, developing panicle, and the early developing florets.
CC {ECO:0000269|PubMed:19688213}.
CC -!- DOMAIN: The first transmembrane domain may act as a type I signal
CC anchor. The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT58885.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAV59304.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF17562.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB488786; BAH24103.1; -; mRNA.
DR EMBL; AC105318; AAV59304.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC119292; AAT58885.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008211; BAF17562.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000142; EEE63844.1; -; Genomic_DNA.
DR RefSeq; XP_015640016.1; XM_015784530.1.
DR AlphaFoldDB; B9FJ61; -.
DR STRING; 39947.B9FJ61; -.
DR MEROPS; A22.A15; -.
DR PaxDb; B9FJ61; -.
DR PRIDE; B9FJ61; -.
DR GeneID; 4338901; -.
DR KEGG; osa:4338901; -.
DR OrthoDB; 1087991at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; B9FJ61; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IBA:GO_Central.
DR GO; GO:0033619; P:membrane protein proteolysis; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR InterPro; IPR007369; Peptidase_A22B_SPP.
DR InterPro; IPR006639; Preselin/SPP.
DR PANTHER; PTHR12174; PTHR12174; 1.
DR Pfam; PF04258; Peptidase_A22B; 1.
DR SMART; SM00730; PSN; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="Signal peptide peptidase 2"
FT /id="PRO_0000419099"
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..89
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..165
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..230
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..290
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 290..292
FT /note="PAL"
FT MOTIF 340..343
FT /note="Endoplasmic reticulum targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT ACT_SITE 239
FT /evidence="ECO:0000250"
SQ SEQUENCE 343 AA; 37973 MW; A92628A8E2786BEB CRC64;
MKTHERAANL ALAGLSLAPL VVKVNPNANV ILTACLAVYV GCYRSVKPTP PAETMSKEHA
MRFPLVGSAM LLSLFLLFKF LSKDLVNTVL TAYFFILGIA ALCATLLPSI KRFLPKEWND
NAIVWRAPLF HSLSVEFTRS QVVASIPGFF FCIWYAAKKH WLANNVLGIS FCIQGIEMLS
LGSFKTGAIL LSGLFFYDIF WVFFTPVMVS VAKSFDAPIK LLFPTGDAAR PFSMLGLGDI
VIPGIFVALA LRFDVSRGIK NRYFNSAFLG YTVGLTVTII VMNWFQAAQP ALLYIVPGVI
GFVAVHCLWN GEVKPLLEYN ESKAEEEEAC EEDTDSKQNK KKE
