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Database: UniProt
Entry: A0A1L8HC98_XENLA
LinkDB: A0A1L8HC98_XENLA
Original site: A0A1L8HC98_XENLA 
ID   A0A1L8HC98_XENLA        Unreviewed;       556 AA.
AC   A0A1L8HC98;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Transmembrane protease serine 2 isoform X1 {ECO:0000313|RefSeq:XP_041437449.1, ECO:0000313|RefSeq:XP_041437450.1};
GN   Name=tmprss2.2.L {ECO:0000313|RefSeq:XP_041437449.1,
GN   ECO:0000313|RefSeq:XP_041437450.1, ECO:0000313|RefSeq:XP_041437451.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_041437451.1};
RN   [1] {ECO:0000313|RefSeq:XP_041437449.1, ECO:0000313|RefSeq:XP_041437450.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_041437449.1,
RC   ECO:0000313|RefSeq:XP_041437450.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_041437449.1,
RC   ECO:0000313|RefSeq:XP_041437450.1};
RG   RefSeq;
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   RefSeq; XP_041437449.1; XM_041581515.1.
DR   RefSeq; XP_041437450.1; XM_041581516.1.
DR   RefSeq; XP_041437451.1; XM_041581517.1.
DR   STRING; 8355.A0A1L8HC98; -.
DR   PaxDb; 8355-A0A1L8HC98; -.
DR   KEGG; xla:495248; -.
DR   OMA; HENWSEN; -.
DR   OrthoDB; 5577980at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
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:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 3.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
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   InterPro; IPR033116; TRYPSIN_SER.
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; 3.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 3.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50068; LDLRA_2; 3.
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   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, ECO:0000256|RuleBase:RU363034};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034};
KW   Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|RefSeq:XP_041437449.1};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        65..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          213..253
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          320..553
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        115..130
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        157..172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        197..212
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   556 AA;  60727 MW;  C96EBC8FD29F0C1C CRC64;
     MDPNVYVVPP SYNEYELPPP PLYEPVPYTI PVKPPPPPYS SEVNTAQFGA GPPTRSSSWT
     HKKKICLISA TVVCTVVAIG AALIIGFLVT KPSNTATCQI RCAYSSKCIS PYQICDGTYD
     CIFGTDEDNC VTKSPSNPTC QIYCIYTFKC IYGYQICDGI RDCTYGDDEN NCVTTRPTYC
     EKSCGSSPSC VLSSQWCDGV TQCPNGEDEM SCVRLYGADF QLQVYSPLKS AWLPVCSNNW
     NNDYGKLACQ DFGYSRSSYN RSDTLPSTYS PNGYFQLNNG SWSSKFYTNV QYSSSCFSGN
     VVSLRCIRCG VSNNNVASRI VGGTNAALGN WPWQVSLRHS SGILCGGSII SPKWIVTAAH
     CVYGSSGIAS DWKVFAGLLN LSNYYDSNGH LVEKIIAHPG YKDSNKDKDI ALMKLRDEIT
     FGYNTQPVCL PNSGMFWNAG TSCWISGWGT TSEKGTVSTT LKNAEVPLID SKVCNQSSMY
     NGEITSSMIC AGYRSGGVDT CQGDSGGPLV TKTSSIWWLV GDTSWGYGCA RVNKPGVYGN
     MTTFLEWIYL QTRINS
//
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