TMPSC_HUMAN
ID TMPSC_HUMAN Reviewed; 348 AA.
AC Q86WS5; B9ZVX2;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Transmembrane protease serine 12;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=TMPRSS12;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-62.
RC TISSUE=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 [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23436708; DOI=10.1002/pmic.201200489;
RA Liu M., Hu Z., Qi L., Wang J., Zhou T., Guo Y., Zeng Y., Zheng B., Wu Y.,
RA Zhang P., Chen X., Tu W., Zhang T., Zhou Q., Jiang M., Guo X., Zhou Z.,
RA Sha J.;
RT "Scanning of novel cancer/testis proteins by human testis proteomic
RT analysis.";
RL Proteomics 13:1200-1210(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In testis, expressed in spermatocytes and
CC spermatids. Expressed in colorectal cancer (at protein level).
CC {ECO:0000269|PubMed:23436708}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AC008121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048112; AAH48112.1; -; mRNA.
DR CCDS; CCDS44881.1; -.
DR RefSeq; NP_872365.1; NM_182559.2.
DR AlphaFoldDB; Q86WS5; -.
DR SMR; Q86WS5; -.
DR BioGRID; 129574; 22.
DR IntAct; Q86WS5; 16.
DR STRING; 9606.ENSP00000381476; -.
DR MEROPS; S01.291; -.
DR GlyGen; Q86WS5; 2 sites.
DR iPTMnet; Q86WS5; -.
DR PhosphoSitePlus; Q86WS5; -.
DR BioMuta; TMPRSS12; -.
DR DMDM; 317373305; -.
DR MassIVE; Q86WS5; -.
DR PaxDb; Q86WS5; -.
DR PeptideAtlas; Q86WS5; -.
DR PRIDE; Q86WS5; -.
DR ProteomicsDB; 70199; -.
DR Antibodypedia; 2710; 75 antibodies from 15 providers.
DR DNASU; 283471; -.
DR Ensembl; ENST00000398458.4; ENSP00000381476.3; ENSG00000186452.11.
DR GeneID; 283471; -.
DR KEGG; hsa:283471; -.
DR MANE-Select; ENST00000398458.4; ENSP00000381476.3; NM_182559.3; NP_872365.2.
DR UCSC; uc001rwx.5; human.
DR CTD; 283471; -.
DR GeneCards; TMPRSS12; -.
DR HGNC; HGNC:28779; TMPRSS12.
DR HPA; ENSG00000186452; Tissue enriched (testis).
DR neXtProt; NX_Q86WS5; -.
DR OpenTargets; ENSG00000186452; -.
DR PharmGKB; PA142670731; -.
DR VEuPathDB; HostDB:ENSG00000186452; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161878; -.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; Q86WS5; -.
DR OMA; HEAEVHY; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q86WS5; -.
DR TreeFam; TF335943; -.
DR PathwayCommons; Q86WS5; -.
DR SignaLink; Q86WS5; -.
DR BioGRID-ORCS; 283471; 11 hits in 1065 CRISPR screens.
DR ChiTaRS; TMPRSS12; human.
DR GenomeRNAi; 283471; -.
DR Pharos; Q86WS5; Tdark.
DR PRO; PR:Q86WS5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86WS5; protein.
DR Bgee; ENSG00000186452; Expressed in sperm and 30 other tissues.
DR ExpressionAtlas; Q86WS5; baseline and differential.
DR Genevisible; Q86WS5; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..348
FT /note="Transmembrane protease serine 12"
FT /id="PRO_0000290438"
FT TOPO_DOM 21..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 78..318
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 24..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 206..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 237..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 264..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 19
FT /note="Y -> H (in dbSNP:rs10876100)"
FT /id="VAR_051848"
FT VARIANT 62
FT /note="E -> K (in dbSNP:rs829121)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051849"
FT VARIANT 127
FT /note="A -> T (in dbSNP:rs861204)"
FT /id="VAR_051850"
SQ SEQUENCE 348 AA; 38605 MW; 1EE2D503ED35B452 CRC64;
MRLGLLSVAL LFVGSSHLYS DHYSPSGRHR LGPSPEPAAS SQQAEAVRKR LRRRREGGAH
AEDCGTAPLK DVLQGSRIIG GTEAQAGAWP WVVSLQIKYG RVLVHVCGGT LVRERWVLTA
AHCTKDASDP LMWTAVIGTN NIHGRYPHTK KIKIKAIIIH PNFILESYVN DIALFHLKKA
VRYNDYIQPI CLPFDVFQIL DGNTKCFISG WGRTKEEGNA TNILQDAEVH YISREMCNSE
RSYGGIIPNT SFCAGDEDGA FDTCRGDSGG PLMCYLPEYK RFFVMGITSY GHGCGRRGFP
GVYIGPSFYQ KWLTEHFFHA STQGILTINI LRGQILIALC FVILLATT
