ID SPPL3_HUMAN Reviewed; 385 AA.
AC Q8TCT6; Q3MJ04; Q8TAU4; Q96DD9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 12-APR-2017, entry version 132.
DE RecName: Full=Signal peptide peptidase-like 3 {ECO:0000303|PubMed:12077416, ECO:0000312|HGNC:HGNC:30424};
DE Short=SPP-like 3 {ECO:0000303|PubMed:12077416};
DE EC=3.4.23.-;
DE AltName: Full=Intramembrane protease 2 {ECO:0000303|PubMed:12139484};
DE Short=IMP-2 {ECO:0000303|PubMed:12139484};
DE AltName: Full=Presenilin homologous protein 1 {ECO:0000303|PubMed:11978763};
DE Short=PSH1 {ECO:0000303|PubMed:11978763};
DE AltName: Full=Presenilin-like protein 4 {ECO:0000303|Ref.1};
GN Name=SPPL3 {ECO:0000303|PubMed:12077416, ECO:0000312|HGNC:HGNC:30424};
GN Synonyms=IMP2 {ECO:0000303|PubMed:12139484}, PSL4 {ECO:0000303|Ref.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M.;
RT "Characterization of a new protein family with homology to
RT presenilins.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=12077416; DOI=10.1126/science.1070925;
RA Weihofen A., Binns K., Lemberg M.K., Ashman K., Martoglio B.;
RT "Identification of signal peptide peptidase, a presenilin-type
RT aspartic protease.";
RL Science 296:2215-2218(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Blood;
RX PubMed=12139484; DOI=10.1023/A:1016365227942;
RA Grigorenko A.P., Moliaka Y.K., Korovaitseva G.I., Rogaev E.I.;
RT "Novel class of polytopic proteins with domains associated with
RT putative protease activity.";
RL Biochemistry (Mosc.) 67:826-834(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RA Kondo K., Heike T., Yorifuji T., Nishikomori R., Kawai M., Ma F.,
RA Ma L., Adachi S., Nakahata T.;
RT "Proteolytic processing, N-glycosylation, and proteasomal degradation
RT of human signal peptide peptidase-like protein 3: the YD and PAL
RT motifs, but not the GXGD motif, are critical for protein stability.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Liver, Pancreas, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-385 (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11978763; DOI=10.1093/hmg/11.9.1037;
RA Ponting C.P., Hutton M., Nyborg A., Baker M., Jansen K., Golde T.E.;
RT "Identification of a novel family of presenilin homologues.";
RL Hum. Mol. Genet. 11:1037-1044(2002).
RN [9]
RP SUBUNIT, TOPOLOGY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND LACK
RP OF GLYCOSYLATION.
RX PubMed=15385547; DOI=10.1074/jbc.M407898200;
RA Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U.,
RA Rovelli G., Martoglio B.;
RT "Consensus analysis of signal peptide peptidase and homologous human
RT aspartic proteases reveals opposite topology of catalytic domains
RT compared with presenilins.";
RL J. Biol. Chem. 279:50790-50798(2004).
RN [10]
RP SUBUNIT, SUBCELLULAR LOCATION, AND LACK OF GLYCOSYLATION.
RX PubMed=15998642; DOI=10.1074/jbc.M501645200;
RA Krawitz P., Haffner C., Fluhrer R., Steiner H., Schmid B., Haass C.;
RT "Differential localization and identification of a critical aspartate
RT suggest non-redundant proteolytic functions of the presenilin
RT homologues SPPL2b and SPPL3.";
RL J. Biol. Chem. 280:39515-39523(2005).
RN [11]
RP FUNCTION, ENZYME REGULATION, AND SUBUNIT.
RX PubMed=16873890; DOI=10.1096/fj.06-5762com;
RA Nyborg A.C., Ladd T.B., Jansen K., Kukar T., Golde T.E.;
RT "Intramembrane proteolytic cleavage by human signal peptide peptidase
RT like 3 and malaria signal peptide peptidase.";
RL FASEB J. 20:1671-1679(2006).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=16829952; DOI=10.1038/ncb1440;
RA Friedmann E., Hauben E., Maylandt K., Schleeger S., Vreugde S.,
RA Lichtenthaler S.F., Kuhn P.H., Stauffer D., Rovelli G., Martoglio B.;
RT "SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in
RT activated dendritic cells to trigger IL-12 production.";
RL Nat. Cell Biol. 8:843-848(2006).
RN [13]
RP FUNCTION, LACK OF ENZYME REGULATION, INTERACTION WITH ENV, AND
RP MUTAGENESIS OF ASP-272.
RX PubMed=23132852; DOI=10.1074/jbc.M112.371369;
RA Voss M., Fukumori A., Kuhn P.H., Kunzel U., Klier B., Grammer G.,
RA Haug-Kroper M., Kremmer E., Lichtenthaler S.F., Steiner H.,
RA Schroder B., Haass C., Fluhrer R.;
RT "Foamy virus envelope protein is a substrate for signal peptide
RT peptidase-like 3 (SPPL3).";
RL J. Biol. Chem. 287:43401-43409(2012).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ASP-201 AND ASP-272.
RX PubMed=25354954; DOI=10.15252/embj.201488375;
RA Voss M., Kunzel U., Higel F., Kuhn P.H., Colombo A., Fukumori A.,
RA Haug-Kroper M., Klier B., Grammer G., Seidl A., Schroder B., Obst R.,
RA Steiner H., Lichtenthaler S.F., Haass C., Fluhrer R.;
RT "Shedding of glycan-modifying enzymes by signal peptide peptidase-like
RT 3 (SPPL3) regulates cellular N-glycosylation.";
RL EMBO J. 33:2890-2905(2014).
RN [15]
RP FUNCTION, AND INTERACTION WITH STIM1.
RX PubMed=25384971; DOI=10.1128/MCB.01124-14;
RA Makowski S.L., Wang Z., Pomerantz J.L.;
RT "A protease-independent function for SPPL3 in NFAT activation.";
RL Mol. Cell. Biol. 35:451-467(2015).
RN [16]
RP FUNCTION.
RX PubMed=25827571; DOI=10.1074/mcp.M115.048298;
RA Kuhn P.H., Voss M., Haug-Kroper M., Schroder B., Schepers U.,
RA Brase S., Haass C., Lichtenthaler S.F., Fluhrer R.;
RT "Secretome analysis identifies novel signal peptide peptidase-like 3
RT (SPPL3) substrates and reveals a role of SPPL3 in multiple Golgi
RT glycosylation pathways.";
RL Mol. Cell. Proteomics 14:1584-1598(2015).
CC -!- FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that
CC cleaves type II membrane protein substrates in or close to their
CC luminal transmembrane domain boundaries (PubMed:16873890,
CC PubMed:25354954, PubMed:25827571). Acts like a sheddase by
CC mediating the proteolytic release and secretion of active site-
CC containing ectodomains of glycan-modifiying glycosidase and
CC glycosyltransferase enzymes such as MGAT5, B4GAT1 and B4GALT1
CC (PubMed:25354954, PubMed:25827571). Catalyzes the intramembrane
CC cleavage of the envelope glycoprotein gp130 and/or the leader
CC peptide gp18LP of the simian foamy virus independent of prior
CC ectodomain shedding by furin or furin-like proprotein convertase
CC (PC)-mediated cleavage proteolysis (PubMed:23132852). May also
CC have the ability to serve as a shedding protease for subsequent
CC intramembrane proteolysis by SPPL2A and SPPL2B of the envelope
CC glycoprotein gp130 (PubMed:23132852). Plays a role in the
CC regulation of cellular glycosylation processes (PubMed:25354954).
CC Required to link T-cell antigen receptor (TCR) and calcineurin-
CC NFAT signaling cascades in lymphocytes by promoting the
CC association of STIM1 and ORAI1 during store-operated calcium entry
CC (SOCE) in a protease-independent manner (PubMed:25384971).
CC {ECO:0000269|PubMed:16873890, ECO:0000269|PubMed:23132852,
CC ECO:0000269|PubMed:25354954, ECO:0000269|PubMed:25384971,
CC ECO:0000269|PubMed:25827571}.
CC -!- ENZYME REGULATION: Its proteolytic activity is blocked by a signal
CC peptide peptidase (SPP) inhibitor, (ZLL)2-ketone (ZLL) or a gamma-
CC secretase inhibitor, LY411,575 (PubMed:16873890). However, is not
CC inhibited by ZLL and LY411,575 for activity on simian foamy virus
CC envelope glycoprotein gp130 (PubMed:23132852).
CC {ECO:0000269|PubMed:16873890, ECO:0000269|PubMed:23132852}.
CC -!- SUBUNIT: Monomer (PubMed:15385547, PubMed:15998642,
CC PubMed:16873890). Homodimer (PubMed:15385547, PubMed:15998642,
CC PubMed:16873890). Interacts with STIM1 (via the transmembrane
CC region and the SOAR/CAD domain); the interaction promotes the
CC binding of STIM1 to ORAI1 (PubMed:25384971). Interacts with the
CC simian foamy virus envelope glycoprotein gp130 and its processed
CC leader peptide gp18LP; preferentially interacts with the envelope
CC glycoprotein gp130 (PubMed:23132852).
CC {ECO:0000250|UniProtKB:Q9CUS9, ECO:0000269|PubMed:15385547,
CC ECO:0000269|PubMed:15998642, ECO:0000269|PubMed:16873890,
CC ECO:0000269|PubMed:23132852, ECO:0000269|PubMed:25384971}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein
CC {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:16829952}.
CC Membrane {ECO:0000269|PubMed:15385547}; Multi-pass membrane
CC protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:15385547}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some
CC isoforms.;
CC Name=1;
CC IsoId=Q8TCT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCT6-2; Sequence=VSP_005206;
CC Name=3;
CC IsoId=Q8TCT6-3; Sequence=VSP_005205;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:15385547). Expressed
CC in the brain (PubMed:11978763). {ECO:0000269|PubMed:11978763,
CC ECO:0000269|PubMed:15385547}.
CC -!- DOMAIN: The first transmembrane domain may act as a type I signal
CC anchor (PubMed:15385547). The catalytic loops is exposed toward
CC the lumen (PubMed:15385547). The PAL motif is required for normal
CC active site conformation. The catalytic domains embedded in the
CC membrane are in the opposite orientation to that of the presenilin
CC protein family (By similarity). {ECO:0000250|UniProtKB:P49768,
CC ECO:0000269|PubMed:15385547}.
CC -!- PTM: Not glycosylated (PubMed:15385547, PubMed:15998642).
CC {ECO:0000269|PubMed:15385547, ECO:0000269|PubMed:15998642}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11290.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR EMBL; AJ345030; CAC87791.1; -; mRNA.
DR EMBL; AJ420898; CAD13135.1; -; mRNA.
DR EMBL; AY169313; AAO12538.1; -; mRNA.
DR EMBL; AB252457; BAF30928.1; -; mRNA.
DR EMBL; CH471054; EAW98220.1; -; Genomic_DNA.
DR EMBL; BC009551; AAH09551.1; -; mRNA.
DR EMBL; BC025781; AAH25781.1; -; mRNA.
DR EMBL; BC073910; AAH73910.1; -; mRNA.
DR EMBL; BC101625; AAI01626.1; -; mRNA.
DR EMBL; BC101627; AAI01628.1; -; mRNA.
DR EMBL; AK074916; BAC11290.1; ALT_INIT; mRNA.
DR CCDS; CCDS9208.1; -. [Q8TCT6-2]
DR RefSeq; NP_620584.2; NM_139015.4. [Q8TCT6-2]
DR UniGene; Hs.507087; -.
DR UniGene; Hs.683964; -.
DR ProteinModelPortal; Q8TCT6; -.
DR BioGrid; 125743; 17.
DR STRING; 9606.ENSP00000288680; -.
DR MEROPS; A22.005; -.
DR SwissPalm; Q8TCT6; -.
DR BioMuta; SPPL3; -.
DR DMDM; 25008979; -.
DR MaxQB; Q8TCT6; -.
DR PaxDb; Q8TCT6; -.
DR PeptideAtlas; Q8TCT6; -.
DR PRIDE; Q8TCT6; -.
DR Ensembl; ENST00000353487; ENSP00000288680; ENSG00000157837. [Q8TCT6-2]
DR GeneID; 121665; -.
DR KEGG; hsa:121665; -.
DR UCSC; uc001tzd.4; human. [Q8TCT6-1]
DR CTD; 121665; -.
DR DisGeNET; 121665; -.
DR GeneCards; SPPL3; -.
DR HGNC; HGNC:30424; SPPL3.
DR HPA; HPA004194; -.
DR HPA; HPA059958; -.
DR MIM; 608240; gene.
DR neXtProt; NX_Q8TCT6; -.
DR OpenTargets; ENSG00000157837; -.
DR eggNOG; KOG2443; Eukaryota.
DR eggNOG; ENOG410XTES; LUCA.
DR GeneTree; ENSGT00530000062920; -.
DR HOGENOM; HOG000243413; -.
DR HOVERGEN; HBG023986; -.
DR InParanoid; Q8TCT6; -.
DR KO; K09598; -.
DR OMA; ELWEGPA; -.
DR OrthoDB; EOG091G0EHF; -.
DR PhylomeDB; Q8TCT6; -.
DR TreeFam; TF323842; -.
DR ChiTaRS; SPPL3; human.
DR GeneWiki; UNQ1887; -.
DR GenomeRNAi; 121665; -.
DR PRO; PR:Q8TCT6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR Bgee; ENSG00000157837; -.
DR ExpressionAtlas; Q8TCT6; baseline and differential.
DR Genevisible; Q8TCT6; HS.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; IDA:UniProtKB.
DR GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0051533; P:positive regulation of NFAT protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Golgi apparatus; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 385 Signal peptide peptidase-like 3.
FT /FTId=PRO_0000073912.
FT TOPO_DOM 1 8 Lumenal. {ECO:0000269|PubMed:15385547}.
FT TRANSMEM 9 29 Helical. {ECO:0000255}.
FT TOPO_DOM 30 75 Cytoplasmic.
FT {ECO:0000269|PubMed:15385547}.
FT TRANSMEM 76 96 Helical. {ECO:0000255}.
FT TOPO_DOM 97 98 Lumenal. {ECO:0000255}.
FT TRANSMEM 99 119 Helical. {ECO:0000255}.
FT TOPO_DOM 120 137 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 138 160 Helical. {ECO:0000255}.
FT TOPO_DOM 161 165 Lumenal. {ECO:0000255}.
FT TRANSMEM 166 186 Helical. {ECO:0000255}.
FT TOPO_DOM 187 191 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 192 212 Helical. {ECO:0000255}.
FT TOPO_DOM 213 263 Lumenal. {ECO:0000269|PubMed:15385547}.
FT TRANSMEM 264 284 Helical. {ECO:0000255}.
FT TOPO_DOM 285 312 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 313 333 Helical. {ECO:0000255}.
FT TOPO_DOM 334 340 Lumenal. {ECO:0000255}.
FT TRANSMEM 341 361 Helical. {ECO:0000255}.
FT TOPO_DOM 362 385 Cytoplasmic.
FT {ECO:0000269|PubMed:15385547}.
FT MOTIF 342 344 PAL.
FT COMPBIAS 375 380 Poly-Ser.
FT ACT_SITE 201 201 {ECO:0000250|UniProtKB:P49810}.
FT ACT_SITE 272 272 {ECO:0000250|UniProtKB:P49810}.
FT VAR_SEQ 1 216 Missing (in isoform 3).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_005205.
FT VAR_SEQ 59 82 EQEPIIGFQPMDSTRARFLPMGAC -> NSTNNSIQTIDST
FT QALFLPIGAS (in isoform 2).
FT {ECO:0000303|PubMed:12077416,
FT ECO:0000303|PubMed:12139484,
FT ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_005206.
FT MUTAGEN 201 201 D->A: Does not affect complex
FT glycosylation pattern of cellular
FT glycoproteins; when associated with A-
FT 272. {ECO:0000269|PubMed:25354954}.
FT MUTAGEN 272 272 D->A: Loss of intramembrane-cleaving
FT activity toward the simian foamy virus
FT envelope glycoprotein gp130. Does not
FT affect complex glycosylation pattern of
FT cellular glycoproteins; when associated
FT with A-201. {ECO:0000269|PubMed:23132852,
FT ECO:0000269|PubMed:25354954}.
FT CONFLICT 140 140 F -> Y (in Ref. 7; BAC11290).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 65 362 ismart:PSN [T]
FT MYHIT 67 373 ipfam:Peptidase_A22B [T]
SQ SEQUENCE 385 AA; 42563 MW; BF829565E14A2996 CRC64;
MAEQTYSWAY SLVDSSQVST FLISILLIVY GSFRSLNMDF ENQDKEKDSN SSSGSFNGEQ
EPIIGFQPMD STRARFLPMG ACVSLLVMFF FFDSVQVVFT ICTAVLATIA FAFLLLPMCQ
YLTRPCSPQN KISFGCCGRF TAAELLSFSL SVMLVLIWVL TGHWLLMDAL AMGLCVAMIA
FVRLPSLKVS CLLLSGLLIY DVFWVFFSAY IFNSNVMVKV ATQPADNPLD VLSRKLHLGP
NVGRDVPRLS LPGKLVFPSS TGSHFSMLGI GDIVMPGLLL CFVLRYDNYK KQASGDSCGA
PGPANISGRM QKVSYFHCTL IGYFVGLLTA TVASRIHRAA QPALLYLVPF TLLPLLTMAY
LKGDLRRMWS EPFHSKSSSS RFLEV
//
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