ID A0A3Q1GDL0_9TELE Unreviewed; 475 AA.
AC A0A3Q1GDL0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Transmembrane serine protease 2 {ECO:0000313|Ensembl:ENSAPOP00000028323.1};
GN Name=TMPRSS2 {ECO:0000313|Ensembl:ENSAPOP00000028323.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000028323.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000028323.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; A0A3Q1GDL0; -.
DR STRING; 80966.ENSAPOP00000028323; -.
DR Ensembl; ENSAPOT00000018463.1; ENSAPOP00000028323.1; ENSAPOG00000013509.1.
DR GeneTree; ENSGT00940000155207; -.
DR InParanoid; A0A3Q1GDL0; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR036055; LDL_receptor-like_sf.
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; 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 PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF11; TRANSMEMBRANE SERINE PROTEASE 2; 1.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..188
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 219..458
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 120..138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 132..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 475 AA; 52517 MW; F532B8888C0EECA4 CRC64;
MPLYCKVPRY REKPAIQRYM GRDRCNSNLE PQFVCKCASS HSVCVVVSDV KQRCVKFTVA
AVICLLLLLL LAGILLAYYC ELLKSCFWRS NLEYTHMLSV CSNTDPCPSV SSPCSRGMRC
GDGSCVWESQ WCNGVMDCPA GQDEAHCVRL HGSSFLLQIY STQTKAWRSV CSHGWTDQQG
RASCQSIGYS RSDAQICNSK SKQIQRVKAG LFSDCGSGIN SSRAPRSSLA SVGSWPWQVS
LQVSGVHRCG GAIVSPYWIV TAAHCVMRTS SPADWSVYAG IMDRLNTLFN PAYSVSHVIM
HEDFNILTRE NDVALMRLSR PLDITASSNI GPVCLPNVGL NVTVPQSYWI TRFDRSRNGD
SGSVQLMEAQ VSVVDTTECN SSIAYNGKIS QDMFCARETE AGARICHADT GGPLVTLTDG
LWWLIGDSIW GEHCTGQKKP GVYGNVTSYL DWIHRHMKVK TNGIHMEGSF NRVYV
//
