SIPL1_ORYSJ
ID SIPL1_ORYSJ Reviewed; 371 AA.
AC Q7G7C7; A0A0P0XUF9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Signal peptide peptidase-like 1;
DE Short=OsSPPL1;
DE EC=3.4.23.-;
GN Name=SPPL1; OrderedLocusNames=Os10g0393100, LOC_Os10g25360;
GN ORFNames=OsJ_31401, OSJNBa0011L09.25;
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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].
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 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}.
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DR EMBL; AC092388; AAM22738.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP53575.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26432.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT10685.1; -; Genomic_DNA.
DR EMBL; CM000147; EAZ15956.1; -; Genomic_DNA.
DR EMBL; AK061008; BAG87672.1; -; mRNA.
DR EMBL; AK072853; BAG93176.1; -; mRNA.
DR RefSeq; XP_015614833.1; XM_015759347.1.
DR AlphaFoldDB; Q7G7C7; -.
DR STRING; 4530.OS10T0393100-01; -.
DR PaxDb; Q7G7C7; -.
DR PRIDE; Q7G7C7; -.
DR EnsemblPlants; Os10t0393100-01; Os10t0393100-01; Os10g0393100.
DR EnsemblPlants; Os10t0393100-02; Os10t0393100-02; Os10g0393100.
DR GeneID; 4348538; -.
DR Gramene; Os10t0393100-01; Os10t0393100-01; Os10g0393100.
DR Gramene; Os10t0393100-02; Os10t0393100-02; Os10g0393100.
DR KEGG; osa:4348538; -.
DR eggNOG; KOG2443; Eukaryota.
DR HOGENOM; CLU_061449_0_0_1; -.
DR InParanoid; Q7G7C7; -.
DR OMA; PCSDGNK; -.
DR OrthoDB; 1087991at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q7G7C7; 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: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 Endosome; Hydrolase; Membrane; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..371
FT /note="Signal peptide peptidase-like 1"
FT /id="PRO_0000419100"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..80
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..149
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..258
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..326
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 328..330
FT /note="PAL"
FT ACT_SITE 186
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /evidence="ECO:0000250"
SQ SEQUENCE 371 AA; 40673 MW; 71D80DE0752B42D9 CRC64;
MESLWKLSYL LEPASLALIL TAVSVAYASA SRALDHGREM ERNLDFSEAS ITLDRSQALM
IPLASSCSLL LMFYLFSSVS HLVTAFTAVA SAMALFFCLS PYVNCVRSRL GVGDPFVSRC
CSKPFTRLQG LLVAICVGTV VAWLVSGHWL LNNLLGISIC IAFVSHVRLP NIKICALLLV
CLFVYDVFWV FFSERFFGAN VMVSVATQKA SNPVHTVANK LSLPGLQLIT KKLELPVKLV
FPRSLMGGLA PGSSPGDYMM LGLGDMAIPG MLLALVLSFD HRKIKDMSVS QDMPPSKQRK
YVWYALTGYG VGLVTALAAG ILSQSPQPAL LYLVPSTLGP VMYMSWLRNE LWELWEGSRP
IINDKAHLLE V
