SIPL5_ARATH
ID SIPL5_ARATH Reviewed; 536 AA.
AC Q9MA44;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Signal peptide peptidase-like 5;
DE Short=AtSPPL5;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=SPPL5; OrderedLocusNames=At1g05820; ORFNames=T20M3.9;
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 [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Flower bud;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9MA44-1; Sequence=Displayed;
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; AB330675; BAF74780.1; -; mRNA.
DR EMBL; AC009999; AAF29388.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27898.1; -; Genomic_DNA.
DR PIR; H86192; H86192.
DR RefSeq; NP_172073.2; NM_100463.3. [Q9MA44-1]
DR AlphaFoldDB; Q9MA44; -.
DR SMR; Q9MA44; -.
DR STRING; 3702.AT1G05820.1; -.
DR MEROPS; A22.A04; -.
DR PaxDb; Q9MA44; -.
DR ProteomicsDB; 234464; -. [Q9MA44-1]
DR EnsemblPlants; AT1G05820.1; AT1G05820.1; AT1G05820. [Q9MA44-1]
DR GeneID; 837092; -.
DR Gramene; AT1G05820.1; AT1G05820.1; AT1G05820. [Q9MA44-1]
DR KEGG; ath:AT1G05820; -.
DR Araport; AT1G05820; -.
DR TAIR; locus:2198733; AT1G05820.
DR eggNOG; KOG2442; Eukaryota.
DR InParanoid; Q9MA44; -.
DR OrthoDB; 535101at2759; -.
DR PhylomeDB; Q9MA44; -.
DR PRO; PR:Q9MA44; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MA44; baseline and differential.
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 Alternative splicing; Endosome; Glycoprotein; Hydrolase; Membrane;
KW Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..536
FT /note="Signal peptide peptidase-like 5"
FT /id="PRO_0000419097"
FT TOPO_DOM 30..186
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..273
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..344
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..428
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 94..170
FT /note="PA"
FT REGION 218..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 491..493
FT /note="PAL"
FT ACT_SITE 384
FT /evidence="ECO:0000250"
FT ACT_SITE 437
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 536 AA; 58728 MW; 4EBE2DFAE766D476 CRC64;
MSLPPFTCRL LAAAAALYLI GLLCVGADTK DVTAPKIPGC SNEFQMVKVE NWVNGENGET
FTAMTAQFGT MLPSDKDKAV KLPVALTTPL DSCSNLTSKL SWSIALSVRG ECAFTVKAQV
AQAGGAAALV LINDKEELDE MVCGEKDTSL NVSIPILMIT TSSGDALKKS IMQNKKVELL
LYAPKSPIVD YAVVFLWLMS VGTVFVASVW SHVTSPKKND EQYDELSPKK SSNVDATKGG
AEEETLDISA MGAVIFVISA STFLVLLFFF MSSWFILILT IFFVIGGMQG MHNINVTLIT
RRCSKCGQKN LKLPLLGNTS ILSLVVLLFC FVVAILWFMN RKTSHAWAGQ DIFGICMMIN
VLQVARLPNI RVATILLCCA FFYDIFWVFI SPLIFKQSVM IAVARGSKDT GESIPMLLRI
PRLSDPWGGY NMIGFGDILF PGLLICFIFR FDKENNKGVS NGYFPWLMFG YGLGLFLTYL
GLYVMNGHGQ PALLYLVPCT LGITVILGLV RKELRDLWNY GTQQPSAADV NPSPEA
