SPPL3_HUMAN
ID SPPL3_HUMAN Reviewed; 384 AA.
AC Q8TCT6; Q3MJ04; Q8TAU4; Q96DD9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 164.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M.;
RT "Characterization of a new protein family with homology to 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 aspartic
RT 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 putative
RT protease activity.";
RL Biochemistry (Mosc.) 67:826-834(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Kondo K., Heike T., Yorifuji T., Nishikomori R., Kawai M., Ma F., Ma L.,
RA Adachi S., Nakahata T.;
RT "Proteolytic processing, N-glycosylation, and proteasomal degradation of
RT human signal peptide peptidase-like protein 3: the YD and PAL motifs, but
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-384 (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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 OF
RP GLYCOSYLATION.
RX PubMed=15385547; DOI=10.1074/jbc.m407898200;
RA Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U., Rovelli G.,
RA Martoglio B.;
RT "Consensus analysis of signal peptide peptidase and homologous human
RT aspartic proteases reveals opposite topology of catalytic domains compared
RT 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 homologues
RT SPPL2b and SPPL3.";
RL J. Biol. Chem. 280:39515-39523(2005).
RN [11]
RP FUNCTION, ACTIVITY 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 like
RT 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 ACTIVITY REGULATION, INTERACTION WITH ENV, AND
RP MUTAGENESIS OF ASP-271.
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., Schroder B.,
RA Haass C., Fluhrer R.;
RT "Foamy virus envelope protein is a substrate for signal peptide peptidase-
RT like 3 (SPPL3).";
RL J. Biol. Chem. 287:43401-43409(2012).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ASP-200 AND ASP-271.
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 3
RT (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., Brase S.,
RA 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 mediating
CC the proteolytic release and secretion of active site-containing
CC ectodomains of glycan-modifiying glycosidase and glycosyltransferase
CC enzymes such as MGAT5, B4GAT1 and B4GALT1 (PubMed:25354954,
CC PubMed:25827571). Catalyzes the intramembrane cleavage of the envelope
CC glycoprotein gp130 and/or the leader peptide gp18LP of the simian foamy
CC virus independent of prior ectodomain shedding by furin or furin-like
CC proprotein convertase (PC)-mediated cleavage proteolysis
CC (PubMed:23132852). May also have the ability to serve as a shedding
CC protease for subsequent intramembrane proteolysis by SPPL2A and SPPL2B
CC of the envelope glycoprotein gp130 (PubMed:23132852). Plays a role in
CC the regulation of cellular glycosylation processes (PubMed:25354954).
CC Required to link T-cell antigen receptor (TCR) and calcineurin-NFAT
CC signaling cascades in lymphocytes by promoting the association of STIM1
CC and ORAI1 during store-operated calcium entry (SOCE) in a protease-
CC independent manner (PubMed:25384971). {ECO:0000269|PubMed:16873890,
CC ECO:0000269|PubMed:23132852, ECO:0000269|PubMed:25354954,
CC ECO:0000269|PubMed:25384971, ECO:0000269|PubMed:25827571}.
CC -!- ACTIVITY 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, PubMed:16873890).
CC Homodimer (PubMed:15385547, PubMed:15998642, PubMed:16873890).
CC Interacts with STIM1 (via the transmembrane region and the SOAR/CAD
CC domain); the interaction promotes the binding of STIM1 to ORAI1
CC (PubMed:25384971). Interacts with the simian foamy virus envelope
CC glycoprotein gp130 and its processed leader peptide gp18LP;
CC preferentially interacts with the envelope glycoprotein gp130
CC (PubMed:23132852). {ECO:0000250|UniProtKB:Q9CUS9,
CC ECO:0000269|PubMed:15385547, ECO:0000269|PubMed:15998642,
CC ECO:0000269|PubMed:16873890, ECO:0000269|PubMed:23132852,
CC 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}. Membrane
CC {ECO:0000269|PubMed:15385547}; Multi-pass membrane protein
CC {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:15385547}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q8TCT6-2; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8TCT6-3; Sequence=VSP_005205;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:15385547). Expressed in
CC 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 the
CC lumen (PubMed:15385547). The PAL motif is required for normal active
CC site conformation. The catalytic domains embedded in the membrane are
CC in the opposite orientation to that of the presenilin protein family
CC (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=Truncated N-terminus.; 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 AlphaFoldDB; Q8TCT6; -.
DR BioGRID; 125743; 57.
DR IntAct; Q8TCT6; 16.
DR STRING; 9606.ENSP00000288680; -.
DR MEROPS; A22.005; -.
DR iPTMnet; Q8TCT6; -.
DR PhosphoSitePlus; Q8TCT6; -.
DR SwissPalm; Q8TCT6; -.
DR BioMuta; SPPL3; -.
DR DMDM; 25008979; -.
DR EPD; Q8TCT6; -.
DR jPOST; Q8TCT6; -.
DR MassIVE; Q8TCT6; -.
DR MaxQB; Q8TCT6; -.
DR PaxDb; Q8TCT6; -.
DR PeptideAtlas; Q8TCT6; -.
DR PRIDE; Q8TCT6; -.
DR ProteomicsDB; 74158; -. [Q8TCT6-2]
DR ProteomicsDB; 74159; -. [Q8TCT6-3]
DR Antibodypedia; 31508; 113 antibodies from 21 providers.
DR DNASU; 121665; -.
DR Ensembl; ENST00000353487.7; ENSP00000288680.4; ENSG00000157837.16. [Q8TCT6-2]
DR GeneID; 121665; -.
DR KEGG; hsa:121665; -.
DR MANE-Select; ENST00000353487.7; ENSP00000288680.4; NM_139015.5; NP_620584.2.
DR UCSC; uc001tzd.4; human. [Q8TCT6-2]
DR CTD; 121665; -.
DR DisGeNET; 121665; -.
DR GeneCards; SPPL3; -.
DR HGNC; HGNC:30424; SPPL3.
DR HPA; ENSG00000157837; Low tissue specificity.
DR MIM; 608240; gene.
DR neXtProt; NX_Q8TCT6; -.
DR OpenTargets; ENSG00000157837; -.
DR VEuPathDB; HostDB:ENSG00000157837; -.
DR eggNOG; KOG2443; Eukaryota.
DR GeneTree; ENSGT00940000158101; -.
DR HOGENOM; CLU_061449_0_0_1; -.
DR InParanoid; Q8TCT6; -.
DR OMA; PCSDGNK; -.
DR PhylomeDB; Q8TCT6; -.
DR TreeFam; TF323842; -.
DR PathwayCommons; Q8TCT6; -.
DR SignaLink; Q8TCT6; -.
DR BioGRID-ORCS; 121665; 39 hits in 1088 CRISPR screens.
DR ChiTaRS; SPPL3; human.
DR GeneWiki; UNQ1887; -.
DR GenomeRNAi; 121665; -.
DR Pharos; Q8TCT6; Tbio.
DR PRO; PR:Q8TCT6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TCT6; protein.
DR Bgee; ENSG00000157837; Expressed in upper arm skin and 187 other tissues.
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:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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: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:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
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; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Membrane; Protease; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..384
FT /note="Signal peptide peptidase-like 3"
FT /id="PRO_0000073912"
FT TOPO_DOM 1..8
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:15385547"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15385547"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..97
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..164
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..262
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:15385547"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..339
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15385547"
FT MOTIF 341..343
FT /note="PAL"
FT ACT_SITE 200
FT /evidence="ECO:0000250|UniProtKB:P49810"
FT ACT_SITE 271
FT /evidence="ECO:0000250|UniProtKB:P49810"
FT VAR_SEQ 1..215
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005205"
FT MUTAGEN 200
FT /note="D->A: Does not affect complex glycosylation pattern
FT of cellular glycoproteins; when associated with A-271."
FT /evidence="ECO:0000269|PubMed:25354954"
FT MUTAGEN 271
FT /note="D->A: Loss of intramembrane-cleaving activity toward
FT the simian foamy virus envelope glycoprotein gp130. Does
FT not affect complex glycosylation pattern of cellular
FT glycoproteins; when associated with A-200."
FT /evidence="ECO:0000269|PubMed:23132852,
FT ECO:0000269|PubMed:25354954"
FT CONFLICT 59..81
FT /note="NSTNNSIQTIDSTQALFLPIGAS -> EQEPIIGFQPMDSTRARFLPMGAC
FT (in Ref. 2; CAD13135)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="F -> Y (in Ref. 7; BAC11290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 42261 MW; 04D8C036355B32A1 CRC64;
MAEQTYSWAY SLVDSSQVST FLISILLIVY GSFRSLNMDF ENQDKEKDSN SSSGSFNGNS
TNNSIQTIDS TQALFLPIGA SVSLLVMFFF FDSVQVVFTI CTAVLATIAF AFLLLPMCQY
LTRPCSPQNK ISFGCCGRFT AAELLSFSLS VMLVLIWVLT GHWLLMDALA MGLCVAMIAF
VRLPSLKVSC LLLSGLLIYD VFWVFFSAYI FNSNVMVKVA TQPADNPLDV LSRKLHLGPN
VGRDVPRLSL PGKLVFPSST GSHFSMLGIG DIVMPGLLLC FVLRYDNYKK QASGDSCGAP
GPANISGRMQ KVSYFHCTLI GYFVGLLTAT VASRIHRAAQ PALLYLVPFT LLPLLTMAYL
KGDLRRMWSE PFHSKSSSSR FLEV
