SIPL5_ORYSJ
ID SIPL5_ORYSJ Reviewed; 542 AA.
AC Q5Z413; A0A0P0X1I0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Signal peptide peptidase-like 5;
DE Short=OsSPPL5;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=SPPL5; OrderedLocusNames=Os06g0730900, LOC_Os06g51430;
GN ORFNames=B1206D04.13, OsJ_22746, OSJNBa0069C14.36;
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=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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
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}.
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DR EMBL; AP005750; BAD62128.1; -; Genomic_DNA.
DR EMBL; AP006616; BAD62487.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20573.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS99650.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE66404.1; -; Genomic_DNA.
DR EMBL; AK062118; BAG88222.1; -; mRNA.
DR EMBL; AK065172; BAG89399.1; -; mRNA.
DR RefSeq; XP_015642991.1; XM_015787505.1.
DR AlphaFoldDB; Q5Z413; -.
DR SMR; Q5Z413; -.
DR STRING; 4530.OS06T0730900-01; -.
DR MEROPS; A22.A05; -.
DR PaxDb; Q5Z413; -.
DR PRIDE; Q5Z413; -.
DR EnsemblPlants; Os06t0730900-01; Os06t0730900-01; Os06g0730900.
DR EnsemblPlants; Os06t0730900-02; Os06t0730900-02; Os06g0730900.
DR EnsemblPlants; Os06t0730900-03; Os06t0730900-03; Os06g0730900.
DR GeneID; 4342150; -.
DR Gramene; Os06t0730900-01; Os06t0730900-01; Os06g0730900.
DR Gramene; Os06t0730900-02; Os06t0730900-02; Os06g0730900.
DR Gramene; Os06t0730900-03; Os06t0730900-03; Os06g0730900.
DR KEGG; osa:4342150; -.
DR eggNOG; KOG2442; Eukaryota.
DR HOGENOM; CLU_023799_4_1_1; -.
DR InParanoid; Q5Z413; -.
DR OMA; MRYDWAG; -.
DR OrthoDB; 535101at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5Z413; 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; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..542
FT /note="Signal peptide peptidase-like 5"
FT /id="PRO_0000419104"
FT TOPO_DOM 24..192
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..275
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..342
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..426
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..486
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 92..167
FT /note="PA"
FT MOTIF 489..491
FT /note="PAL"
FT ACT_SITE 382
FT /evidence="ECO:0000250"
FT ACT_SITE 435
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 542 AA; 59696 MW; 7739781FC84237A0 CRC64;
MAAATAAVFA LLMASALAGA AAGGDIVHHD DEAPKIPGCS NDFILVKVQS WVNGKEDDEY
VGVGARFGPQ IVSKEKHANR TRLMLADPID CCTSPKEKVS GDILLVQRGK CKFTKKAKFA
EAAGASGIII INHVHELYKM VCEKNETDLD INIPAVLLPR DAGFALHTVL TSGNSVSVQQ
YSPDRPVVDT AEVFLWLMAV GTVLCASYWS AWSAREALCE QEKLLKDGRE VLLNVENGSS
SGMIDINVAS AIMFVVVASC FLIMLYKMMS SWFVELLVVI FCVGGVEGLQ TCLVALLSRW
FRAASESFFK VPFFGAVSYL TLAVSPFCIV FAVLWAVHRH FTYAWIGQDI LGIALIITVI
QIVRVPNLKV GSVLLSCAFF YDIFWVFVSK RWFHESVMIV VARGDKTDED GVPMLLKIPR
MFDPWGGYSI IGFGDILLPG LLVAFALRYD WAAKKSLQTG YFLWSMVAYG SGLLITYVAL
NLMDGHGQPA LLYIVPFTLG ALISLGWKRG ELWNLWSKGE PERVCPHHMH MQPQPKTPPL
VQ
