TMPSD_HUMAN
ID TMPSD_HUMAN Reviewed; 586 AA.
AC Q9BYE2; B4DTM9; E9PIJ5; E9PRA0; F8WAJ3; J3KQC6; Q1RMF8; Q86YM4; Q96JY8;
AC Q9BYE1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 5.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Transmembrane protease serine 13;
DE EC=3.4.21.-;
DE AltName: Full=Membrane-type mosaic serine protease;
DE Short=Mosaic serine protease;
GN Name=TMPRSS13; Synonyms=MSP, TMPRSS11;
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] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY,
RP POLYMORPHISM, AND VARIANTS ALA-SER-PRO-ALA-GLN-73 INS AND 74-ALA--GLN-78
RP DEL.
RC TISSUE=Lung;
RX PubMed=11267681; DOI=10.1016/s0167-4781(01)00184-1;
RA Kim D.R., Sharmin S., Inoue M., Kido H.;
RT "Cloning and expression of novel mosaic serine proteases with and without a
RT transmembrane domain from human lung.";
RL Biochim. Biophys. Acta 1518:204-209(2001).
RN [2]
RP SEQUENCE REVISION TO 192; 259; 298 AND 496.
RA Kim D.R., Inoue M., Kido H.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT 74-ALA--GLN-78 DEL.
RA Park T.J., Park W.J.;
RT "Homo sapiens transmembrane protease, serine 6 (TMPRSS6) mRNA.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), AND VARIANT
RP 74-ALA--GLN-78 DEL.
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=MSPL {ECO:0000303|PubMed:11267681};
CC IsoId=Q9BYE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BYE2-2; Sequence=VSP_013103, VSP_013104;
CC Name=3; Synonyms=MSPS {ECO:0000303|PubMed:11267681};
CC IsoId=Q9BYE2-3; Sequence=VSP_013099, VSP_013102;
CC Name=4;
CC IsoId=Q9BYE2-4; Sequence=VSP_013100, VSP_013101;
CC Name=6;
CC IsoId=Q9BYE2-6; Sequence=VSP_013102;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are predominantly expressed
CC in lung, placenta, pancreas, and prostate. Isoform 3 is weakly
CC expressed in testis and peripheral blood lymphocytes.
CC {ECO:0000269|PubMed:11267681}.
CC -!- POLYMORPHISM: The repeat A-S-P-A-[GLQR] is polymorphic and the number
CC of copies varies between 12 to 14. {ECO:0000269|PubMed:11267681}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Was termed TMPRSS6 (Ref.3). {ECO:0000305}.
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DR EMBL; AB048796; BAB39741.2; -; mRNA.
DR EMBL; AB048797; BAB39742.2; -; mRNA.
DR EMBL; AY190317; AAO38062.1; -; mRNA.
DR EMBL; AK027798; BAB55376.1; -; mRNA.
DR EMBL; AK300283; BAG62041.1; -; mRNA.
DR EMBL; AP002962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114928; AAI14929.1; -; mRNA.
DR CCDS; CCDS41721.1; -. [Q9BYE2-6]
DR CCDS; CCDS55788.1; -. [Q9BYE2-3]
DR CCDS; CCDS55789.1; -. [Q9BYE2-4]
DR CCDS; CCDS58185.1; -. [Q9BYE2-2]
DR RefSeq; NP_001070731.1; NM_001077263.2. [Q9BYE2-6]
DR RefSeq; NP_001193718.1; NM_001206789.1. [Q9BYE2-3]
DR RefSeq; NP_001193719.1; NM_001206790.1. [Q9BYE2-4]
DR RefSeq; NP_001231924.1; NM_001244995.1. [Q9BYE2-2]
DR AlphaFoldDB; Q9BYE2; -.
DR SMR; Q9BYE2; -.
DR BioGRID; 123845; 140.
DR IntAct; Q9BYE2; 3.
DR STRING; 9606.ENSP00000434279; -.
DR MEROPS; S01.087; -.
DR TCDB; 8.A.131.1.13; the transmembrane protease serine 3 (tmprss3) family.
DR GlyGen; Q9BYE2; 4 sites.
DR iPTMnet; Q9BYE2; -.
DR PhosphoSitePlus; Q9BYE2; -.
DR SwissPalm; Q9BYE2; -.
DR BioMuta; TMPRSS13; -.
DR DMDM; 313104278; -.
DR jPOST; Q9BYE2; -.
DR MassIVE; Q9BYE2; -.
DR PaxDb; Q9BYE2; -.
DR PeptideAtlas; Q9BYE2; -.
DR PRIDE; Q9BYE2; -.
DR ProteomicsDB; 20829; -.
DR ProteomicsDB; 23254; -.
DR ProteomicsDB; 30511; -.
DR ProteomicsDB; 79624; -. [Q9BYE2-1]
DR ProteomicsDB; 79625; -. [Q9BYE2-2]
DR ProteomicsDB; 79626; -. [Q9BYE2-3]
DR ProteomicsDB; 79627; -. [Q9BYE2-4]
DR Antibodypedia; 32401; 91 antibodies from 17 providers.
DR DNASU; 84000; -.
DR Ensembl; ENST00000430170.6; ENSP00000387702.2; ENSG00000137747.16. [Q9BYE2-2]
DR Ensembl; ENST00000445164.6; ENSP00000394114.2; ENSG00000137747.16. [Q9BYE2-1]
DR Ensembl; ENST00000524993.6; ENSP00000434279.1; ENSG00000137747.16. [Q9BYE2-6]
DR Ensembl; ENST00000526090.1; ENSP00000436502.1; ENSG00000137747.16. [Q9BYE2-4]
DR Ensembl; ENST00000528626.5; ENSP00000435813.1; ENSG00000137747.16. [Q9BYE2-3]
DR GeneID; 84000; -.
DR KEGG; hsa:84000; -.
DR MANE-Select; ENST00000524993.6; ENSP00000434279.1; NM_001077263.3; NP_001070731.1. [Q9BYE2-6]
DR UCSC; uc001pru.3; human. [Q9BYE2-1]
DR CTD; 84000; -.
DR DisGeNET; 84000; -.
DR GeneCards; TMPRSS13; -.
DR HGNC; HGNC:29808; TMPRSS13.
DR HPA; ENSG00000137747; Tissue enhanced (esophagus, skin).
DR MIM; 610050; gene.
DR neXtProt; NX_Q9BYE2; -.
DR OpenTargets; ENSG00000137747; -.
DR PharmGKB; PA142670732; -.
DR VEuPathDB; HostDB:ENSG00000137747; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159197; -.
DR HOGENOM; CLU_006842_19_2_1; -.
DR InParanoid; Q9BYE2; -.
DR OMA; FRAPCMS; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF351678; -.
DR PathwayCommons; Q9BYE2; -.
DR SignaLink; Q9BYE2; -.
DR BioGRID-ORCS; 84000; 11 hits in 1065 CRISPR screens.
DR ChiTaRS; TMPRSS13; human.
DR GenomeRNAi; 84000; -.
DR Pharos; Q9BYE2; Tbio.
DR PRO; PR:Q9BYE2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BYE2; protein.
DR Bgee; ENSG00000137747; Expressed in upper arm skin and 132 other tissues.
DR ExpressionAtlas; Q9BYE2; baseline and differential.
DR Genevisible; Q9BYE2; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.10.250.10; -; 1.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR017327; Peptidase_S1A_TMPRSS13.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF037935; TMPRSS13; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Protease; Reference proteome; Repeat; Serine protease; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..586
FT /note="Transmembrane protease serine 13"
FT /id="PRO_0000088698"
FT TOPO_DOM 1..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..586
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 9..13
FT /note="1-1"
FT REPEAT 14..18
FT /note="2-1; approximate"
FT REPEAT 19..23
FT /note="1-2"
FT REPEAT 24..28
FT /note="1-3"
FT REPEAT 29..33
FT /note="2-2"
FT REPEAT 34..38
FT /note="1-4"
FT REPEAT 39..43
FT /note="1-5"
FT REPEAT 44..48
FT /note="1-6"
FT REPEAT 49..53
FT /note="2-3"
FT REPEAT 54..58
FT /note="1-7"
FT REPEAT 59..63
FT /note="1-8"
FT REPEAT 64..68
FT /note="2-4"
FT REPEAT 69..78
FT /note="1-9; approximate"
FT REPEAT 79..83
FT /note="1-10"
FT REPEAT 84..88
FT /note="1-11"
FT REPEAT 89..93
FT /note="1-12"
FT DOMAIN 195..325
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 204..226
FT /note="LDL-receptor class A"
FT DOMAIN 326..559
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 9..93
FT /note="13 X 5 AA repeats of A-S-P-A-[GLQR]"
FT REGION 14..68
FT /note="4 X 5 AA repeats of T-P-P-G-R"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 366
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 414
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 511
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 250..314
FT /evidence="ECO:0000250"
FT DISULFID 263..317
FT /evidence="ECO:0000250"
FT DISULFID 351..367
FT /evidence="ECO:0000250"
FT DISULFID 448..517
FT /evidence="ECO:0000250"
FT DISULFID 480..496
FT /evidence="ECO:0000250"
FT DISULFID 507..535
FT /evidence="ECO:0000250"
FT VAR_SEQ 151..186
FT /note="GTSLPKFTWREGQKQLPLIGCVLLLIALVVSLIILF -> V (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11267681,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_013099"
FT VAR_SEQ 428..491
FT /note="AHIHPACLPMHGQTFSLNETCWITGFGKTRETDDKTSPFLREVQVNLIDFKK
FT CNDYLVYDSYLT -> GEGICTPRSPAPQPQHPLQPSHLSASVNSYPGPKASAGQKSKT
FT LKDPYMEHFCFIIRETEAQGL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013100"
FT VAR_SEQ 492..586
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013101"
FT VAR_SEQ 560..586
FT /note="VRSLQQDTAPSRLGTSSGGDPGGAPRL -> SEVRFRKS (in isoform
FT 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11267681,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013102"
FT VAR_SEQ 560..563
FT /note="VRSL -> SSAG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_013103"
FT VAR_SEQ 564..586
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_013104"
FT VARIANT 73
FT /note="R -> RASPAQ"
FT /evidence="ECO:0000303|PubMed:11267681"
FT /id="VAR_081354"
FT VARIANT 74..78
FT /note="Missing"
FT /evidence="ECO:0000303|PubMed:11267681,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VAR_081355"
FT CONFLICT 192
FT /note="H -> Y (in Ref. 3; AAO38062)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> E (in Ref. 3; AAO38062)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="C -> R (in Ref. 3; AAO38062)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="D -> G (in Ref. 4; BAG62041)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="L -> V (in Ref. 1; BAB39741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 63167 MW; EDA2E3B7509FB1C6 CRC64;
MERDSHGNAS PARTPSAGAS PAQASPAGTP PGRASPAQAS PAQASPAGTP PGRASPAQAS
PAGTPPGRAS PGRASPAQAS PAQASPARAS PALASLSRSS SGRSSSARSA SVTTSPTRVY
LVRATPVGAV PIRSSPARSA PATRATRESP GTSLPKFTWR EGQKQLPLIG CVLLLIALVV
SLIILFQFWQ GHTGIRYKEQ RESCPKHAVR CDGVVDCKLK SDELGCVRFD WDKSLLKIYS
GSSHQWLPIC SSNWNDSYSE KTCQQLGFES AHRTTEVAHR DFANSFSILR YNSTIQESLH
RSECPSQRYI SLQCSHCGLR AMTGRIVGGA LASDSKWPWQ VSLHFGTTHI CGGTLIDAQW
VLTAAHCFFV TREKVLEGWK VYAGTSNLHQ LPEAASIAEI IINSNYTDEE DDYDIALMRL
SKPLTLSAHI HPACLPMHGQ TFSLNETCWI TGFGKTRETD DKTSPFLREV QVNLIDFKKC
NDYLVYDSYL TPRMMCAGDL RGGRDSCQGD SGGPLVCEQN NRWYLAGVTS WGTGCGQRNK
PGVYTKVTEV LPWIYSKMEV RSLQQDTAPS RLGTSSGGDP GGAPRL
