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Minor histocompatibility antigen H13 (EC 3.4.23.-) (Intramembrane protease 1) (IMP-1) (IMPAS-1) (hIMP1) (Presenilin-like protein 3) (Signal peptide peptidase)

 HM13_HUMAN              Reviewed;         377 AA.
Q8TCT9; B2RAY5; E1P5L3; Q15K36; Q540H8; Q5JWP2; Q5JWP3; Q5JWP4;
Q5JWP5; Q7Z4F2; Q86Y35; Q95H87; Q9H110; Q9H111;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 155.
RecName: Full=Minor histocompatibility antigen H13;
EC=3.4.23.-;
AltName: Full=Intramembrane protease 1;
Short=IMP-1;
Short=IMPAS-1;
Short=hIMP1;
AltName: Full=Presenilin-like protein 3;
AltName: Full=Signal peptide peptidase;
Name=HM13; Synonyms=H13, IMP1, PSL3, SPP; ORFNames=MSTP086;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 62-73;
128-136; 137-161; 242-251 AND 338-352, FUNCTION, TOPOLOGY,
GLYCOSYLATION, AND MUTAGENESIS OF ASN-10; ASN-20 AND ASP-265.
TISSUE=Cervix carcinoma;
PubMed=12077416; DOI=10.1126/science.1070925;
Weihofen A., Binns K., Lemberg M.K., Ashman K., Martoglio B.;
"Identification of signal peptide peptidase, a presenilin-type
aspartic protease.";
Science 296:2215-2218(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=12972007; DOI=10.1016/S1567-133X(03)00094-2;
Urny J., Hermans-Borgmeyer I., Gercken G., Chica Schaller H.;
"Expression of the presenilin-like signal peptide peptidase (SPP) in
mouse adult brain and during development.";
Gene Expr. Patterns 3:685-691(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), AND TISSUE
SPECIFICITY.
TISSUE=Blood, and Hippocampus;
PubMed=12139484; DOI=10.1023/A:1016365227942;
Grigorenko A.P., Moliaka Y.K., Korovaitseva G.I., Rogaev E.I.;
"Novel class of polytopic proteins with domains associated with
putative protease activity.";
Biochemistry (Mosc.) 67:826-834(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=16730383; DOI=10.1016/j.bbaexp.2006.02.007;
Urny J., Hermans-Borgmeyer I., Schaller H.C.;
"Cell-surface expression of a new splice variant of the mouse signal
peptide peptidase.";
Biochim. Biophys. Acta 1759:159-165(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M.;
"Characterization of a new protein family with homology to
presenilins.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Brown A.C., Roopenian D.C.;
"Genomic analysis of the H13 minor histocompatibility antigen gene.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Aorta;
Liu Y.Q., Gong J., Yu L.T., Sheng H., Qin B.M., Zhao B., Liu B.,
Wang X.Y., Zhang Q., Song L., Gao Y., Zhang C.L., Ye J., Ji X.J.,
Liu B.H., Lu H., Xu H.S., Chen J.Z., Cai M.Q., Zheng W.Y., Teng C.Y.,
Liu Q., Lin J., Zhang A.M., Gao R.L., Hui R.T.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary gland, Retinoblastoma, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
FUNCTION.
PubMed=11714810; DOI=10.4049/jimmunol.167.11.6441;
Lemberg M.K., Bland F.A., Weihofen A., Braud V.M., Martoglio B.;
"Intramembrane proteolysis of signal peptides: an essential step in
the generation of HLA-E epitopes.";
J. Immunol. 167:6441-6446(2001).
[13]
FUNCTION.
PubMed=12145199; DOI=10.1093/emboj/cdf414;
McLauchlan J., Lemberg M.K., Hope G., Martoglio B.;
"Intramembrane proteolysis promotes trafficking of hepatitis C virus
core protein to lipid droplets.";
EMBO J. 21:3980-3988(2002).
[14]
FUNCTION, AND MUTAGENESIS OF ASP-219; GLY-264; ASP-265 AND PRO-317.
PubMed=14741365; DOI=10.1016/S0014-5793(03)01489-3;
Moliaka Y.K., Grigorenko A., Madera D., Rogaev E.I.;
"Impas 1 possesses endoproteolytic activity against multipass membrane
protein substrate cleaving the presenilin 1 holoprotein.";
FEBS Lett. 557:185-192(2004).
[15]
SUBUNIT, TOPOLOGY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=15385547; DOI=10.1074/jbc.M407898200;
Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U.,
Rovelli G., Martoglio B.;
"Consensus analysis of signal peptide peptidase and homologous human
aspartic proteases reveals opposite topology of catalytic domains
compared with presenilins.";
J. Biol. Chem. 279:50790-50798(2004).
[16]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15998642; DOI=10.1074/jbc.M501645200;
Krawitz P., Haffner C., Fluhrer R., Steiner H., Schmid B., Haass C.;
"Differential localization and identification of a critical aspartate
suggest non-redundant proteolytic functions of the presenilin
homologues SPPL2b and SPPL3.";
J. Biol. Chem. 280:39515-39523(2005).
[17]
INTERACTION WITH RNF139.
PubMed=19720873; DOI=10.1083/jcb.200906110;
Stagg H.R., Thomas M., van den Boomen D., Wiertz E.J., Drabkin H.A.,
Gemmill R.M., Lehner P.J.;
"The TRC8 E3 ligase ubiquitinates MHC class I molecules before
dislocation from the ER.";
J. Cell Biol. 186:685-692(2009).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-10 AND ASN-20.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION IN CLEAVAGE OF XBP1, INTERACTION WITH DERL1; RNF139 AND XBP1,
AND MUTAGENESIS OF ASP-265.
PubMed=25239945; DOI=10.15252/embj.201488208;
Chen C.Y., Malchus N.S., Hehn B., Stelzer W., Avci D., Langosch D.,
Lemberg M.K.;
"Signal peptide peptidase functions in ERAD to cleave the unfolded
protein response regulator XBP1u.";
EMBO J. 33:2492-2506(2014).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Catalyzes intramembrane proteolysis of some signal
peptides after they have been cleaved from a preprotein, resulting
in the release of the fragment from the ER membrane into the
cytoplasm. Required to generate lymphocyte cell surface (HLA-E)
epitopes derived from MHC class I signal peptides
(PubMed:11714810). May be necessary for the removal of the signal
peptide that remains attached to the hepatitis C virus core
protein after the initial proteolytic processing of the
polyprotein (PubMed:12145199). Involved in the intramembrane
cleavage of the integral membrane protein PSEN1 (PubMed:12077416,
PubMed:11714810, PubMed:14741365). Cleaves the integral membrane
protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner
(PubMed:25239945). May play a role in graft rejection (By
similarity). {ECO:0000250|UniProtKB:Q9D8V0,
ECO:0000269|PubMed:11714810, ECO:0000269|PubMed:12077416,
ECO:0000269|PubMed:12145199, ECO:0000269|PubMed:14741365,
ECO:0000269|PubMed:25239945}.
-!- SUBUNIT: Monomer (PubMed:15385547, PubMed:15998642). Homodimer
(PubMed:15385547, PubMed:15998642). Interacts with RNF139
(PubMed:19720873, PubMed:25239945). Interacts with DERL1 and XBP1
isoform 1 (PubMed:25239945). {ECO:0000269|PubMed:15385547,
ECO:0000269|PubMed:15998642, ECO:0000269|PubMed:19720873,
ECO:0000269|PubMed:25239945}.
-!- INTERACTION:
Q9BUN8:DERL1; NbExp=6; IntAct=EBI-347472, EBI-398977;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-347472, EBI-741037;
P07237:P4HB; NbExp=3; IntAct=EBI-347472, EBI-395883;
Q8WU17:RNF139; NbExp=2; IntAct=EBI-347472, EBI-1551681;
P17861-1:XBP1; NbExp=2; IntAct=EBI-347472, EBI-7631279;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15998642}; Multi-pass membrane protein
{ECO:0000305}. Membrane {ECO:0000269|PubMed:12077416,
ECO:0000269|PubMed:15385547}; Multi-pass membrane protein
{ECO:0000305}; Lumenal side {ECO:0000269|PubMed:12077416,
ECO:0000269|PubMed:15385547}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane
{ECO:0000250|UniProtKB:Q9D8V0}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q9D8V0}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8TCT9-1; Sequence=Displayed;
Name=2;
IsoId=Q8TCT9-2; Sequence=VSP_005196;
Name=4;
IsoId=Q8TCT9-4; Sequence=VSP_015083;
Name=5;
IsoId=Q8TCT9-5; Sequence=VSP_015082;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in
kidney, liver, placenta, lung, leukocytes and small intestine and
reduced expression in heart and skeletal muscle. Expressed
abundantly in the CNS with highest levels in thalamus and medulla.
{ECO:0000269|PubMed:12139484, ECO:0000269|PubMed:12972007}.
-!- DOMAIN: The first transmembrane domain may act as a type I signal
anchor (PubMed:12077416, PubMed:15385547). The PAL motif is
required for normal active site conformation (By similarity).
{ECO:0000250|UniProtKB:P49768, ECO:0000269|PubMed:12077416,
ECO:0000269|PubMed:15385547}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12077416,
ECO:0000269|PubMed:15385547, ECO:0000269|PubMed:19159218}.
-!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAQ13609.1; Type=Frameshift; Positions=320, 329, 330, 358; Evidence={ECO:0000305};
Sequence=BAC11138.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=CAI19152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI20173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AJ420895; CAD13132.1; -; mRNA.
EMBL; AF515663; AAN77099.1; -; mRNA.
EMBL; AY169310; AAO12535.1; -; mRNA.
EMBL; AY169311; AAO12536.1; -; mRNA.
EMBL; AY169312; AAO12537.1; -; mRNA.
EMBL; DQ168450; ABA56163.1; -; mRNA.
EMBL; AJ345029; CAC87790.1; -; mRNA.
EMBL; AF483215; AAM22076.1; -; mRNA.
EMBL; AF172086; AAQ13609.1; ALT_FRAME; mRNA.
EMBL; AK074686; BAC11138.1; ALT_SEQ; mRNA.
EMBL; AK075283; BAC11519.1; -; mRNA.
EMBL; AK314410; BAG37032.1; -; mRNA.
EMBL; AL110115; CAI20173.1; ALT_SEQ; Genomic_DNA.
EMBL; AL121751; CAI20173.1; JOINED; Genomic_DNA.
EMBL; AL110115; CAI20174.1; -; Genomic_DNA.
EMBL; AL121751; CAI20174.1; JOINED; Genomic_DNA.
EMBL; AL110115; CAI20175.2; -; Genomic_DNA.
EMBL; AL121751; CAI20175.2; JOINED; Genomic_DNA.
EMBL; AL121751; CAI19152.1; ALT_SEQ; Genomic_DNA.
EMBL; AL110115; CAI19152.1; JOINED; Genomic_DNA.
EMBL; AL121751; CAI19153.1; -; Genomic_DNA.
EMBL; AL110115; CAI19153.1; JOINED; Genomic_DNA.
EMBL; AL121751; CAI19154.2; -; Genomic_DNA.
EMBL; AL110115; CAI19154.2; JOINED; Genomic_DNA.
EMBL; CH471077; EAW76436.1; -; Genomic_DNA.
EMBL; CH471077; EAW76437.1; -; Genomic_DNA.
EMBL; CH471077; EAW76435.1; -; Genomic_DNA.
EMBL; CH471077; EAW76438.1; -; Genomic_DNA.
EMBL; BC008938; AAH08938.1; -; mRNA.
EMBL; BC008959; AAH08959.1; -; mRNA.
EMBL; BC062595; AAH62595.1; -; mRNA.
CCDS; CCDS13182.1; -. [Q8TCT9-1]
CCDS; CCDS13183.1; -. [Q8TCT9-4]
CCDS; CCDS42861.1; -. [Q8TCT9-2]
RefSeq; NP_110416.1; NM_030789.3. [Q8TCT9-1]
RefSeq; NP_848695.1; NM_178580.2. [Q8TCT9-4]
RefSeq; NP_848696.1; NM_178581.2. [Q8TCT9-2]
RefSeq; NP_848697.1; NM_178582.2.
UniGene; Hs.373741; -.
ProteinModelPortal; Q8TCT9; -.
BioGrid; 123505; 27.
IntAct; Q8TCT9; 25.
MINT; MINT-3034232; -.
MEROPS; A22.003; -.
iPTMnet; Q8TCT9; -.
PhosphoSitePlus; Q8TCT9; -.
SwissPalm; Q8TCT9; -.
DMDM; 25008563; -.
EPD; Q8TCT9; -.
MaxQB; Q8TCT9; -.
PeptideAtlas; Q8TCT9; -.
PRIDE; Q8TCT9; -.
TopDownProteomics; Q8TCT9-1; -. [Q8TCT9-1]
TopDownProteomics; Q8TCT9-5; -. [Q8TCT9-5]
DNASU; 81502; -.
Ensembl; ENST00000335574; ENSP00000335294; ENSG00000101294. [Q8TCT9-4]
Ensembl; ENST00000340852; ENSP00000343032; ENSG00000101294. [Q8TCT9-1]
Ensembl; ENST00000398174; ENSP00000381237; ENSG00000101294. [Q8TCT9-2]
GeneID; 81502; -.
KEGG; hsa:81502; -.
UCSC; uc002wwb.3; human. [Q8TCT9-1]
CTD; 81502; -.
DisGeNET; 81502; -.
EuPathDB; HostDB:ENSG00000101294.16; -.
GeneCards; HM13; -.
HGNC; HGNC:16435; HM13.
HPA; HPA045089; -.
HPA; HPA056062; -.
MIM; 607106; gene.
neXtProt; NX_Q8TCT9; -.
OpenTargets; ENSG00000101294; -.
PharmGKB; PA29314; -.
GeneTree; ENSGT00530000062920; -.
HOVERGEN; HBG024161; -.
InParanoid; Q8TCT9; -.
KO; K09595; -.
OMA; WWVFGTE; -.
OrthoDB; EOG091G0AWL; -.
PhylomeDB; Q8TCT9; -.
TreeFam; TF105854; -.
ChiTaRS; HM13; human.
GeneWiki; HM13; -.
GenomeRNAi; 81502; -.
PRO; PR:Q8TCT9; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101294; -.
ExpressionAtlas; Q8TCT9; baseline and differential.
Genevisible; Q8TCT9; HS.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ParkinsonsUK-UCL.
GO; GO:0030660; C:Golgi-associated vesicle membrane; IBA:GO_Central.
GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
GO; GO:1904211; P:membrane protein proteolysis involved in retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
GO; GO:0051289; P:protein homotetramerization; TAS:ParkinsonsUK-UCL.
InterPro; IPR007369; Peptidase_A22B_SPP.
InterPro; IPR006639; Preselin/SPP.
PANTHER; PTHR12174; PTHR12174; 1.
Pfam; PF04258; Peptidase_A22B; 1.
SMART; SM00730; PSN; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
Hydrolase; Membrane; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 377 Minor histocompatibility antigen H13.
/FTId=PRO_0000073907.
TOPO_DOM 1 31 Lumenal. {ECO:0000269|PubMed:12077416,
ECO:0000269|PubMed:15385547}.
TRANSMEM 32 52 Helical. {ECO:0000255}.
TOPO_DOM 53 77 Cytoplasmic. {ECO:0000255}.
TRANSMEM 78 98 Helical. {ECO:0000255}.
TOPO_DOM 99 100 Lumenal. {ECO:0000255}.
TRANSMEM 101 121 Helical. {ECO:0000255}.
TOPO_DOM 122 157 Cytoplasmic. {ECO:0000255}.
TRANSMEM 158 178 Helical. {ECO:0000255}.
TOPO_DOM 179 181 Lumenal. {ECO:0000255}.
TRANSMEM 182 202 Helical. {ECO:0000255}.
TOPO_DOM 203 209 Cytoplasmic. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TOPO_DOM 231 256 Lumenal. {ECO:0000269|PubMed:15385547}.
TRANSMEM 257 277 Helical. {ECO:0000255}.
TOPO_DOM 278 290 Cytoplasmic. {ECO:0000255}.
TRANSMEM 291 311 Helical. {ECO:0000255}.
TOPO_DOM 312 314 Lumenal. {ECO:0000255}.
TRANSMEM 315 335 Helical. {ECO:0000255}.
TOPO_DOM 336 377 Cytoplasmic.
{ECO:0000269|PubMed:15385547}.
MOTIF 317 319 PAL.
ACT_SITE 219 219 {ECO:0000250|UniProtKB:P49810}.
ACT_SITE 265 265 {ECO:0000250|UniProtKB:P49810}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 10 10 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 20 20 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 181 222 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_015082.
VAR_SEQ 347 347 E -> ESSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAG
PRRRRPQNPSAIYE (in isoform 2).
{ECO:0000303|PubMed:12139484}.
/FTId=VSP_005196.
VAR_SEQ 348 377 ESNPKDPAAVTESKEGTEASASKGLEKKEK -> SSAEILP
HTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAM
(in isoform 4).
{ECO:0000303|PubMed:12139484,
ECO:0000303|PubMed:16730383}.
/FTId=VSP_015083.
VARIANT 259 259 A -> P (in dbSNP:rs1044419).
/FTId=VAR_014274.
MUTAGEN 10 10 N->Q: Abolishes N-glycosylation; when
associated with Q-20.
{ECO:0000269|PubMed:12077416}.
MUTAGEN 20 20 N->Q: Abolishes N-glycosylation; when
associated with Q-10.
{ECO:0000269|PubMed:12077416}.
MUTAGEN 219 219 D->A: Abolishes proteolysis of PSEN1.
{ECO:0000269|PubMed:14741365}.
MUTAGEN 264 264 G->A: No effect on proteolysis of PSEN1.
{ECO:0000269|PubMed:14741365}.
MUTAGEN 265 265 D->A: No effect on inhibitor binding;
abolishes catalytic activity. Abolishes
proteolysis of PSEN1. Abolishes
proteolysis of XBP1 isoform 1 and
increases interaction with XBP1 isoform
1. {ECO:0000269|PubMed:12077416,
ECO:0000269|PubMed:14741365,
ECO:0000269|PubMed:25239945}.
MUTAGEN 317 317 P->L: Abolishes proteolysis of PSEN1.
{ECO:0000269|PubMed:14741365}.
CONFLICT 132 132 S -> N (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 150 150 K -> R (in Ref. 8; BAC11519).
{ECO:0000305}.
CONFLICT 159 159 D -> A (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 235 235 S -> F (in Ref. 11; AAH08938/AAH08959).
{ECO:0000305}.
CONFLICT 295 295 F -> Y (in Ref. 7; AAQ13609).
{ECO:0000305}.
SEQUENCE 377 AA; 41488 MW; 322D231B52B33118 CRC64;
MDSALSDPHN GSAEAGGPTN STTRPPSTPE GIALAYGSLL LMALLPIFFG ALRSVRCARG
KNASDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY INLLLSMYFF VLGILALSHT
ISPFMNKFFP ASFPNRQYQL LFTQGSGENK EEIINYEFDT KDLVCLGLSS IVGVWYLLRK
HWIANNLFGL AFSLNGVELL HLNNVSTGCI LLGGLFIYDV FWVFGTNVMV TVAKSFEAPI
KLVFPQDLLE KGLEANNFAM LGLGDVVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF
GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV TEMFSYEESN PKDPAAVTES
KEGTEASASK GLEKKEK


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