SIPL3_ARATH
ID SIPL3_ARATH Reviewed; 540 AA.
AC Q4V3B8; Q9ZW87;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Signal peptide peptidase-like 3;
DE Short=AtSPPL3;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=SPPL3; OrderedLocusNames=At2g43070; ORFNames=F14B2, MLF8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18067581; DOI=10.1111/j.1742-4658.2007.06170.x;
RA Tamura T., Asakura T., Uemura T., Ueda T., Terauchi K., Misaka T., Abe K.;
RT "Signal peptide peptidase and its homologs in Arabidopsis thaliana - plant
RT tissue-specific expression and distinct subcellular localization.";
RL FEBS J. 275:34-43(2008).
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:0000269|PubMed:18067581};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18067581}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18067581}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the shoot meristem and root epidermal
CC cells in germinating seeds. {ECO:0000269|PubMed:18067581}.
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=AAM14939.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15159.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004450; AAM14939.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006224; AAM15159.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10205.1; -; Genomic_DNA.
DR EMBL; BT023438; AAY56429.1; -; mRNA.
DR EMBL; AK229438; BAF01298.1; -; mRNA.
DR PIR; F84861; F84861.
DR RefSeq; NP_001318409.1; NM_001337011.1.
DR AlphaFoldDB; Q4V3B8; -.
DR SMR; Q4V3B8; -.
DR BioGRID; 4246; 1.
DR IntAct; Q4V3B8; 1.
DR STRING; 3702.AT2G43070.1; -.
DR MEROPS; A22.A06; -.
DR PaxDb; Q4V3B8; -.
DR PRIDE; Q4V3B8; -.
DR ProteomicsDB; 234563; -.
DR EnsemblPlants; AT2G43070.1; AT2G43070.1; AT2G43070.
DR GeneID; 818909; -.
DR Gramene; AT2G43070.1; AT2G43070.1; AT2G43070.
DR KEGG; ath:AT2G43070; -.
DR Araport; AT2G43070; -.
DR TAIR; locus:2040971; AT2G43070.
DR eggNOG; KOG2442; Eukaryota.
DR HOGENOM; CLU_023799_4_1_1; -.
DR InParanoid; Q4V3B8; -.
DR PhylomeDB; Q4V3B8; -.
DR PRO; PR:Q4V3B8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q4V3B8; baseline and differential.
DR Genevisible; Q4V3B8; AT.
DR GO; GO:0005768; C:endosome; TAS:UniProtKB.
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:0000325; C:plant-type vacuole; HDA:TAIR.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..540
FT /note="Signal peptide peptidase-like 3"
FT /id="PRO_0000419095"
FT TOPO_DOM 29..194
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..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..429
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..492
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 98..172
FT /note="PA"
FT MOTIF 494..496
FT /note="PAL"
FT ACT_SITE 387
FT /evidence="ECO:0000250"
FT ACT_SITE 440
FT /evidence="ECO:0000250"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 540 AA; 59224 MW; F0A7322880A7477D CRC64;
MSSFDPPNHR YSALVLILLL LGFSVAAADD VSWTEDSSLE SPGCTNKFQM VKVLNWVDGV
EGDFLTGLTA QFGAALPSVP DQALRFPAAF VDPLDSCSHL SSRLDGHIAL SIRGNCAFTE
KAKHAEAAGA SALLVINDKE DLDEMGCMEK DTSLNVSIPV LMISKSSGDA LNKSMVDNKN
VELLLYAPKR PAVDLTAGLL LLMAVGTVVV ASLWSELTDP DQANESYSIL AKDVSSAGTR
KDDPEKEILD ISVTGAVFFI VTASIFLLLL FYFMSSWFVW VLTIFFCIGG MQGMHNIIMA
VILRKCRHLA RKSVKLPLLG TMSVLSLLVN IVCLAFAVFW FIKRHTSYSW VGQDILGICL
MITALQVVRL PNIKVATVLL CCAFVYDIFW VFISPLIFHE SVMIVVAQGD SSTGESIPML
LRIPRFFDPW GGYDMIGFGD ILFPGLLISF ASRYDKIKKR VISNGYFLWL TIGYGIGLLL
TYLGLYLMDG HGQPALLYIV PCTLGLAVIL GLVRGELKEL WNYGIEESES HTPEDPMPVA
