HM13_HUMAN
ID HM13_HUMAN Reviewed; 377 AA.
AC Q8TCT9; B2RAY5; E1P5L3; Q15K36; Q540H8; Q5JWP2; Q5JWP3; Q5JWP4; Q5JWP5;
AC Q7Z4F2; Q86Y35; Q95H87; Q9H110; Q9H111;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Minor histocompatibility antigen H13;
DE EC=3.4.23.-;
DE AltName: Full=Intramembrane protease 1;
DE Short=IMP-1;
DE Short=IMPAS-1;
DE Short=hIMP1;
DE AltName: Full=Presenilin-like protein 3;
DE AltName: Full=Signal peptide peptidase;
GN Name=HM13; Synonyms=H13, IMP1, PSL3, SPP; ORFNames=MSTP086;
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 1), PROTEIN SEQUENCE OF 62-73; 128-136;
RP 137-161; 242-251 AND 338-352, FUNCTION, TOPOLOGY, GLYCOSYLATION, AND
RP MUTAGENESIS OF ASN-10; ASN-20 AND ASP-265.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=12972007; DOI=10.1016/s1567-133x(03)00094-2;
RA Urny J., Hermans-Borgmeyer I., Gercken G., Chica Schaller H.;
RT "Expression of the presenilin-like signal peptide peptidase (SPP) in mouse
RT adult brain and during development.";
RL Gene Expr. Patterns 3:685-691(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), AND TISSUE SPECIFICITY.
RC TISSUE=Blood, and Hippocampus;
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 4).
RX PubMed=16730383; DOI=10.1016/j.bbaexp.2006.02.007;
RA Urny J., Hermans-Borgmeyer I., Schaller H.C.;
RT "Cell-surface expression of a new splice variant of the mouse signal
RT peptide peptidase.";
RL Biochim. Biophys. Acta 1759:159-165(2006).
RN [5]
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 presenilins.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Brown A.C., Roopenian D.C.;
RT "Genomic analysis of the H13 minor histocompatibility antigen gene.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Liu Y.Q., Gong J., Yu L.T., Sheng H., Qin B.M., Zhao B., Liu B., Wang X.Y.,
RA Zhang Q., Song L., Gao Y., Zhang C.L., Ye J., Ji X.J., Liu B.H., Lu H.,
RA Xu H.S., Chen J.Z., Cai M.Q., Zheng W.Y., Teng C.Y., Liu Q., Lin J.,
RA Zhang A.M., Gao R.L., Hui R.T.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland, Retinoblastoma, and Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Muscle;
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 [12]
RP FUNCTION.
RX PubMed=11714810; DOI=10.4049/jimmunol.167.11.6441;
RA Lemberg M.K., Bland F.A., Weihofen A., Braud V.M., Martoglio B.;
RT "Intramembrane proteolysis of signal peptides: an essential step in the
RT generation of HLA-E epitopes.";
RL J. Immunol. 167:6441-6446(2001).
RN [13]
RP FUNCTION.
RX PubMed=12145199; DOI=10.1093/emboj/cdf414;
RA McLauchlan J., Lemberg M.K., Hope G., Martoglio B.;
RT "Intramembrane proteolysis promotes trafficking of hepatitis C virus core
RT protein to lipid droplets.";
RL EMBO J. 21:3980-3988(2002).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ASP-219; GLY-264; ASP-265 AND PRO-317.
RX PubMed=14741365; DOI=10.1016/s0014-5793(03)01489-3;
RA Moliaka Y.K., Grigorenko A., Madera D., Rogaev E.I.;
RT "Impas 1 possesses endoproteolytic activity against multipass membrane
RT protein substrate cleaving the presenilin 1 holoprotein.";
RL FEBS Lett. 557:185-192(2004).
RN [15]
RP SUBUNIT, TOPOLOGY, SUBCELLULAR LOCATION, AND 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 [16]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
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 [17]
RP INTERACTION WITH RNF139.
RX PubMed=19720873; DOI=10.1083/jcb.200906110;
RA Stagg H.R., Thomas M., van den Boomen D., Wiertz E.J., Drabkin H.A.,
RA Gemmill R.M., Lehner P.J.;
RT "The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation
RT from the ER.";
RL J. Cell Biol. 186:685-692(2009).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-10 AND ASN-20.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP FUNCTION IN CLEAVAGE OF XBP1, INTERACTION WITH DERL1; RNF139 AND XBP1, AND
RP MUTAGENESIS OF ASP-265.
RX PubMed=25239945; DOI=10.15252/embj.201488208;
RA Chen C.Y., Malchus N.S., Hehn B., Stelzer W., Avci D., Langosch D.,
RA Lemberg M.K.;
RT "Signal peptide peptidase functions in ERAD to cleave the unfolded protein
RT response regulator XBP1u.";
RL EMBO J. 33:2492-2506(2014).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Catalyzes intramembrane proteolysis of some signal peptides
CC after they have been cleaved from a preprotein, resulting in the
CC release of the fragment from the ER membrane into the cytoplasm.
CC Required to generate lymphocyte cell surface (HLA-E) epitopes derived
CC from MHC class I signal peptides (PubMed:11714810). May be necessary
CC for the removal of the signal peptide that remains attached to the
CC hepatitis C virus core protein after the initial proteolytic processing
CC of the polyprotein (PubMed:12145199). Involved in the intramembrane
CC cleavage of the integral membrane protein PSEN1 (PubMed:12077416,
CC PubMed:11714810, PubMed:14741365). Cleaves the integral membrane
CC protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner
CC (PubMed:25239945). May play a role in graft rejection (By similarity).
CC {ECO:0000250|UniProtKB:Q9D8V0, ECO:0000269|PubMed:11714810,
CC ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:12145199,
CC ECO:0000269|PubMed:14741365, ECO:0000269|PubMed:25239945}.
CC -!- SUBUNIT: Monomer (PubMed:15385547, PubMed:15998642). Homodimer
CC (PubMed:15385547, PubMed:15998642). Interacts with RNF139
CC (PubMed:19720873, PubMed:25239945). Interacts with DERL1 and XBP1
CC isoform 1 (PubMed:25239945). {ECO:0000269|PubMed:15385547,
CC ECO:0000269|PubMed:15998642, ECO:0000269|PubMed:19720873,
CC ECO:0000269|PubMed:25239945}.
CC -!- INTERACTION:
CC Q8TCT9; Q9BUN8: DERL1; NbExp=6; IntAct=EBI-347472, EBI-398977;
CC Q8TCT9; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-347472, EBI-741037;
CC Q8TCT9; P07237: P4HB; NbExp=3; IntAct=EBI-347472, EBI-395883;
CC Q8TCT9; Q8WU17: RNF139; NbExp=2; IntAct=EBI-347472, EBI-1551681;
CC Q8TCT9; P17861-1: XBP1; NbExp=2; IntAct=EBI-347472, EBI-7631279;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein
CC {ECO:0000305}. Membrane {ECO:0000269|PubMed:12077416,
CC ECO:0000269|PubMed:15385547}; Multi-pass membrane protein
CC {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:12077416,
CC ECO:0000269|PubMed:15385547}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane
CC {ECO:0000250|UniProtKB:Q9D8V0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9D8V0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TCT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCT9-2; Sequence=VSP_005196;
CC Name=4;
CC IsoId=Q8TCT9-4; Sequence=VSP_015083;
CC Name=5;
CC IsoId=Q8TCT9-5; Sequence=VSP_015082;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in kidney,
CC liver, placenta, lung, leukocytes and small intestine and reduced
CC expression in heart and skeletal muscle. Expressed abundantly in the
CC CNS with highest levels in thalamus and medulla.
CC {ECO:0000269|PubMed:12139484, ECO:0000269|PubMed:12972007}.
CC -!- DOMAIN: The first transmembrane domain may act as a type I signal
CC anchor (PubMed:12077416, PubMed:15385547). The PAL motif is required
CC for normal active site conformation (By similarity).
CC {ECO:0000250|UniProtKB:P49768, ECO:0000269|PubMed:12077416,
CC ECO:0000269|PubMed:15385547}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12077416,
CC ECO:0000269|PubMed:15385547, ECO:0000269|PubMed:19159218}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13609.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC11138.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AJ420895; CAD13132.1; -; mRNA.
DR EMBL; AF515663; AAN77099.1; -; mRNA.
DR EMBL; AY169310; AAO12535.1; -; mRNA.
DR EMBL; AY169311; AAO12536.1; -; mRNA.
DR EMBL; AY169312; AAO12537.1; -; mRNA.
DR EMBL; DQ168450; ABA56163.1; -; mRNA.
DR EMBL; AJ345029; CAC87790.1; -; mRNA.
DR EMBL; AF483215; AAM22076.1; -; mRNA.
DR EMBL; AF172086; AAQ13609.1; ALT_FRAME; mRNA.
DR EMBL; AK074686; BAC11138.1; ALT_SEQ; mRNA.
DR EMBL; AK075283; BAC11519.1; -; mRNA.
DR EMBL; AK314410; BAG37032.1; -; mRNA.
DR EMBL; AL110115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76436.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76437.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76435.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76438.1; -; Genomic_DNA.
DR EMBL; BC008938; AAH08938.1; -; mRNA.
DR EMBL; BC008959; AAH08959.1; -; mRNA.
DR EMBL; BC062595; AAH62595.1; -; mRNA.
DR CCDS; CCDS13182.1; -. [Q8TCT9-1]
DR CCDS; CCDS13183.1; -. [Q8TCT9-4]
DR CCDS; CCDS42861.1; -. [Q8TCT9-2]
DR RefSeq; NP_110416.1; NM_030789.3. [Q8TCT9-1]
DR RefSeq; NP_848695.1; NM_178580.2. [Q8TCT9-4]
DR RefSeq; NP_848696.1; NM_178581.2. [Q8TCT9-2]
DR RefSeq; NP_848697.1; NM_178582.2.
DR AlphaFoldDB; Q8TCT9; -.
DR BioGRID; 123505; 136.
DR IntAct; Q8TCT9; 44.
DR MINT; Q8TCT9; -.
DR ChEMBL; CHEMBL4523407; -.
DR DrugBank; DB00277; Theophylline.
DR MEROPS; A22.003; -.
DR TCDB; 1.A.54.3.5; the presenilin er ca(2+) leak channel (presenilin) family.
DR GlyGen; Q8TCT9; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TCT9; -.
DR MetOSite; Q8TCT9; -.
DR PhosphoSitePlus; Q8TCT9; -.
DR SwissPalm; Q8TCT9; -.
DR BioMuta; HM13; -.
DR DMDM; 25008563; -.
DR CPTAC; CPTAC-1612; -.
DR EPD; Q8TCT9; -.
DR jPOST; Q8TCT9; -.
DR MassIVE; Q8TCT9; -.
DR MaxQB; Q8TCT9; -.
DR PeptideAtlas; Q8TCT9; -.
DR PRIDE; Q8TCT9; -.
DR ProteomicsDB; 74165; -. [Q8TCT9-1]
DR ProteomicsDB; 74166; -. [Q8TCT9-2]
DR ProteomicsDB; 74167; -. [Q8TCT9-4]
DR ProteomicsDB; 74168; -. [Q8TCT9-5]
DR TopDownProteomics; Q8TCT9-1; -. [Q8TCT9-1]
DR TopDownProteomics; Q8TCT9-5; -. [Q8TCT9-5]
DR Antibodypedia; 25181; 141 antibodies from 21 providers.
DR DNASU; 81502; -.
DR Ensembl; ENST00000335574.10; ENSP00000335294.5; ENSG00000101294.18. [Q8TCT9-4]
DR Ensembl; ENST00000340852.9; ENSP00000343032.5; ENSG00000101294.18. [Q8TCT9-1]
DR Ensembl; ENST00000398174.9; ENSP00000381237.3; ENSG00000101294.18. [Q8TCT9-2]
DR Ensembl; ENST00000674240.1; ENSP00000501423.1; ENSG00000101294.18. [Q8TCT9-4]
DR GeneID; 81502; -.
DR KEGG; hsa:81502; -.
DR MANE-Select; ENST00000398174.9; ENSP00000381237.3; NM_178581.3; NP_848696.1. [Q8TCT9-2]
DR UCSC; uc002wwb.3; human. [Q8TCT9-1]
DR CTD; 81502; -.
DR DisGeNET; 81502; -.
DR GeneCards; HM13; -.
DR HGNC; HGNC:16435; HM13.
DR HPA; ENSG00000101294; Low tissue specificity.
DR MIM; 607106; gene.
DR neXtProt; NX_Q8TCT9; -.
DR OpenTargets; ENSG00000101294; -.
DR PharmGKB; PA29314; -.
DR VEuPathDB; HostDB:ENSG00000101294; -.
DR GeneTree; ENSGT00940000156478; -.
DR HOGENOM; CLU_023799_0_0_1; -.
DR InParanoid; Q8TCT9; -.
DR OMA; LFSYEDH; -.
DR OrthoDB; 1087991at2759; -.
DR PhylomeDB; Q8TCT9; -.
DR TreeFam; TF105854; -.
DR PathwayCommons; Q8TCT9; -.
DR Reactome; R-HSA-9707587; Regulation of HMOX1 expression and activity.
DR SignaLink; Q8TCT9; -.
DR BioGRID-ORCS; 81502; 38 hits in 1079 CRISPR screens.
DR ChiTaRS; HM13; human.
DR GeneWiki; HM13; -.
DR GenomeRNAi; 81502; -.
DR Pharos; Q8TCT9; Tbio.
DR PRO; PR:Q8TCT9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8TCT9; protein.
DR Bgee; ENSG00000101294; Expressed in body of pancreas and 179 other tissues.
DR ExpressionAtlas; Q8TCT9; baseline and differential.
DR Genevisible; Q8TCT9; HS.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
DR GO; GO:1904211; P:membrane protein proteolysis involved in retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0061960; P:regulation of heme oxygenase activity; TAS:Reactome.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..377
FT /note="Minor histocompatibility antigen H13"
FT /id="PRO_0000073907"
FT TOPO_DOM 1..31
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:12077416,
FT ECO:0000269|PubMed:15385547"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..100
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..256
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:15385547"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..314
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15385547"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 317..319
FT /note="PAL"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000250|UniProtKB:P49810"
FT ACT_SITE 265
FT /evidence="ECO:0000250|UniProtKB:P49810"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 181..222
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_015082"
FT VAR_SEQ 347
FT /note="E -> ESSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSA
FT IYE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12139484"
FT /id="VSP_005196"
FT VAR_SEQ 348..377
FT /note="ESNPKDPAAVTESKEGTEASASKGLEKKEK -> SSAEILPHTPRLTHFPTV
FT SGSPASLADSMQQKLAGPRRRRPQNPSAM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12139484,
FT ECO:0000303|PubMed:16730383"
FT /id="VSP_015083"
FT VARIANT 259
FT /note="A -> P (in dbSNP:rs1044419)"
FT /id="VAR_014274"
FT MUTAGEN 10
FT /note="N->Q: Abolishes N-glycosylation; when associated
FT with Q-20."
FT /evidence="ECO:0000269|PubMed:12077416"
FT MUTAGEN 20
FT /note="N->Q: Abolishes N-glycosylation; when associated
FT with Q-10."
FT /evidence="ECO:0000269|PubMed:12077416"
FT MUTAGEN 219
FT /note="D->A: Abolishes proteolysis of PSEN1."
FT /evidence="ECO:0000269|PubMed:14741365"
FT MUTAGEN 264
FT /note="G->A: No effect on proteolysis of PSEN1."
FT /evidence="ECO:0000269|PubMed:14741365"
FT MUTAGEN 265
FT /note="D->A: No effect on inhibitor binding; abolishes
FT catalytic activity. Abolishes proteolysis of PSEN1.
FT Abolishes proteolysis of XBP1 isoform 1 and increases
FT interaction with XBP1 isoform 1."
FT /evidence="ECO:0000269|PubMed:12077416,
FT ECO:0000269|PubMed:14741365, ECO:0000269|PubMed:25239945"
FT MUTAGEN 317
FT /note="P->L: Abolishes proteolysis of PSEN1."
FT /evidence="ECO:0000269|PubMed:14741365"
FT CONFLICT 132
FT /note="S -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="K -> R (in Ref. 8; BAC11519)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="D -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="S -> F (in Ref. 11; AAH08938/AAH08959)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="F -> Y (in Ref. 7; AAQ13609)"
FT /evidence="ECO:0000305"
SQ 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
