SIPL1_ARATH
ID SIPL1_ARATH Reviewed; 372 AA.
AC Q93Z32; Q9SZB8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Signal peptide peptidase-like 1;
DE Short=AtSPPL1;
DE EC=3.4.23.-;
GN Name=SPPL1; OrderedLocusNames=At4g33410; ORFNames=F17M5.170;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 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=CAB38799.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80058.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035678; CAB38799.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161583; CAB80058.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86221.1; -; Genomic_DNA.
DR EMBL; AY058181; AAL25595.1; -; mRNA.
DR EMBL; BT000484; AAN18053.1; -; mRNA.
DR PIR; T05992; T05992.
DR RefSeq; NP_567918.1; NM_119495.3.
DR AlphaFoldDB; Q93Z32; -.
DR STRING; 3702.AT4G33410.1; -.
DR MEROPS; A22.A14; -.
DR PaxDb; Q93Z32; -.
DR PRIDE; Q93Z32; -.
DR ProteomicsDB; 234560; -.
DR EnsemblPlants; AT4G33410.1; AT4G33410.1; AT4G33410.
DR GeneID; 829478; -.
DR Gramene; AT4G33410.1; AT4G33410.1; AT4G33410.
DR KEGG; ath:AT4G33410; -.
DR Araport; AT4G33410; -.
DR TAIR; locus:2119236; AT4G33410.
DR eggNOG; KOG2443; Eukaryota.
DR HOGENOM; CLU_061449_0_0_1; -.
DR InParanoid; Q93Z32; -.
DR OMA; PCSDGNK; -.
DR OrthoDB; 1087991at2759; -.
DR PhylomeDB; Q93Z32; -.
DR PRO; PR:Q93Z32; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93Z32; baseline and differential.
DR Genevisible; Q93Z32; AT.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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:0005802; C:trans-Golgi network; 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 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..372
FT /note="Signal peptide peptidase-like 1"
FT /id="PRO_0000419093"
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..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..81
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..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..257
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..325
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..372
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 372 AA; 41002 MW; F9DB75FB9DBB4117 CRC64;
METLWTLLYL LEPAPATLIV TAVTVTFASA FRALNYGKEM ERNRDFSEAS ITLDSSQALM
IPVMSSCSLL LMFYLFSSVS QLLTAFTAIA SVSSLFYWLS PYAVYMKTQL GLSDPFLSRC
CSKSFTRIQG LLLVACAMTV VAWLISGHWV LNNLLGISIC IAFVSHVRLP NIKICAMLLV
CLFVYDIFWV FFSERFFGAN VMVAVATQQA SNPVHTVANS LNLPGLQLIT KKLELPVKIV
FPRNLLGGVV PGVSASDFMM LGLGDMAIPA MLLALVLCFD HRKTRDVVNI FDLKSSKGHK
YIWYALPGYA IGLVAALAAG VLTHSPQPAL LYLVPSTLGP VIFMSWRRKD LAELWEGPAL
SNPIEKSHEI EI
