TMPRSS13
entrez
84000
canonical
uniprot
Q9BYE2
canonical
ensembl
ENSG00000137747
resolver
ensp
ENSP00000387702
resolver
ensp
ENSP00000434279
resolver
ensp
ENSP00000435813
resolver
ensp
ENSP00000436502
resolver
genesymbol
TMPRSS13
resolver
genesymbol_syn
MSP
resolver
genesymbol_syn
TMPRSS11
resolver
hgnc
HGNC:29808
resolver
uniprot
B4DTM9
resolver
uniprot
E9PIJ5
resolver
uniprot
E9PRA0
resolver
uniprot
F8WAJ3
resolver
uniprot
J3KQC6
resolver
uniprot
Q1RMF8
resolver
uniprot
Q86YM4
resolver
uniprot
Q96JY8
resolver
uniprot
Q9BYE1
resolver
uniprot_entry
TMPSD_HUMAN
resolver
uniprot_sec
B4DTM9
resolver
uniprot_sec
E9PIJ5
resolver
uniprot_sec
E9PRA0
resolver
uniprot_sec
F8WAJ3
resolver
uniprot_sec
J3KQC6
resolver
uniprot_sec
Q1RMF8
resolver
uniprot_sec
Q86YM4
resolver
uniprot_sec
Q96JY8
resolver
uniprot_sec
Q9BYE1
resolver
activity_regulation
ACTIVITY REGULATION: Cleavage of HGF is inhibited by SPINT1/HAI-1 via the BPTI/Kunitz inhibitor 1 domain. {ECO:0000269|PubMed:20977675}.
uniprot
proteins
amino_acid_sequence
MERDSHGNASPARTPSAGASPAQASPAGTPPGRASPAQASPAQASPAGTPPGRASPAQASPAGTPPGRASPGRASPAQASPAQASPARASPALASLSRSSSGRSSSARSASVTTSPTRVYLVRATPVGAVPIRSSPARSAPATRATRESPGTSLPKFTWREGQKQLPLIGCVLLLIALVVSLIILFQFWQGHTGIRYKEQRESCPKHAVRCDGVVDCKLKSDELGCVRFDWDKSLLKIYSGSSHQWLPICSSNWNDSYSEKTCQQLGFESAHRTTEVAHRDFANSFSILRYNSTIQESLHRSECPSQRYISLQCSHCGLRAMTGRIVGGALASDSKWPWQVSLHFGTTHICGGTLIDAQWVLTAAHCFFVTREKVLEGWKVYAGTSNLHQLPEAASIAEIIINSNYTDEEDDYDIALMRLSKPLTLSAHIHPACLPMHGQTFSLNETCWITGFGKTRETDDKTSPFLREVQVNLIDFKKCNDYLVYDSYLTPRMMCAGDLRGGRDSCQGDSGGPLVCEQNNRWYLAGVTSWGTGCGQRNKPGVYTKVTEVLPWIYSKMEVRSLQQDTAPSRLGTSSGGDPGGAPRL
uniprot
proteins
ec_number
3.4.21.-
uniprot
proteins
function
FUNCTION: Serine protease (PubMed:20977675, PubMed:28710277, PubMed:34562451). Cleaves the proform of PRSS8/prostasin to form the active protein (PubMed:34562451). Cleaves the proform of HGF to form the active protein which promotes MAPK signaling (PubMed:20977675). Promotes the formation of the stratum corneum and subsequently the epidermal barrier in embryos (By similarity). {ECO:0000250|UniProtKB:Q5U405, ECO:0000269|PubMed:20977675, ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451}.
uniprot
proteins
mass_dalton
63167
uniprot
proteins
mutagenesis
MUTAGEN 196; /note="R->Q: No effect on autocleavage."; /evidence="ECO:0000269|PubMed:35796294"; MUTAGEN 201; /note="R->Q: No effect on autocleavage."; /evidence="ECO:0000269|PubMed:35796294"; MUTAGEN 210; /note="R->Q: No effect on autocleavage."; /evidence="ECO:0000269|PubMed:35796294"; MUTAGEN 228; /note="R->Q: Significantly reduces autocleavage and cleavage of substrates. Abolishes phosphorylation when inhibited by SPINT2/HAI-2, also reduces localization to the cell surface and is instead localized to the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:35796294"; MUTAGEN 255; /note="N->Q: No effect on autocleavage. No effect on PRSS8 cleavage and activation."; /evidence="ECO:0000269|PubMed:34562451"; MUTAGEN 292; /note="N->Q: No effect on autocleavage. No effect on PRSS8 cleavage and activation."; /evidence="ECO:0000269|PubMed:34562451"; MUTAGEN 325; /note="R->Q: Abolishes autocleavage. Abolishes PRSS8 cleavage and activation. Increases localization to the cell surface. No effect on glycosylation."; /evidence="ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451, ECO:0000269|PubMed:35796294"; MUTAGEN 405; /note="N->Q: Loss of localization to the cell surface even in the presence of the inhibitor SPINT2. Reduces PRSS8 cleavage and activation. No effect on interaction with SPINT2."; /evidence="ECO:0000269|PubMed:34562451"; MUTAGEN 445; /note="N->Q: Reduces autocleavage. Loss of localization to the cell surface even in the presence of the inhibitor SPINT2. Reduces PRSS8 cleavage and activation. No effect on interaction with SPINT2."; /evidence="ECO:0000269|PubMed:34562451"; MUTAGEN 511; /note="S->A: Abolishes autocleavage. Abolishes serine protease activity including PRSS8 cleavage and activation. Increases localization to the cell surface. No effect on glycosylation."; /evidence="ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451, ECO:0000269|PubMed:35796294
uniprot
proteins
post_translational_modification
PTM: The inactive zymogen is post-translationally modified and then trafficked to the cell surface, whereby it undergoes autocatalytic cleavage resulting in an activated form that is released extracellularly. {ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451}.; PTM: Phosphorylation is required for localization at the cell surface (PubMed:28710277, PubMed:34562451). Phosphorylation increases following inhibition of protease activity by SPINT2/HAI-2 (PubMed:35796294). {ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451, ECO:0000269|PubMed:35796294}.; PTM: N-glycosylation of Asn-405 and Asn-445 is required for exit from the endoplasmic reticulum and trafficking to the cell surface (PubMed:28710277, PubMed:34562451). Also required for autocleavage of the zymogen, activation and secretion of the mature protein (PubMed:34562451). {ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
11267681
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
20977675
uniprot
proteins
pubmed
28710277
uniprot
proteins
pubmed
34562451
uniprot
proteins
pubmed
35796294
uniprot
proteins
sequence_length
586
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451, ECO:0000269|PubMed:35796294}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:35796294}. Cytoplasm {ECO:0000269|PubMed:28710277}. Note=The non-phosphorylated, inactive full length protein localizes intracellularly (PubMed:28710277). N-glycosylation and phosphorylation is required for trafficking to the cell surface (PubMed:28710277, PubMed:34562451, PubMed:35796294). Interaction with SPINT1/HAI-1 and SPINT2/HAI-2 facilitate its translocation to the cell surface (PubMed:34562451, PubMed:35796294). Proteolytic cleavage is required for secretion (PubMed:35796294). {ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451, ECO:0000269|PubMed:35796294}.
uniprot
proteins
transmembrane_region
TRANSMEM 166..186; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins