ID A0A3Q0CLU8_MESAU Unreviewed; 1243 AA.
AC A0A3Q0CLU8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Polyserase-2 {ECO:0000313|RefSeq:XP_021081671.1};
GN Name=Prss36 {ECO:0000313|RefSeq:XP_021081671.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021081671.1};
RN [1] {ECO:0000313|RefSeq:XP_021081671.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_021081671.1; XM_021226012.1.
DR AlphaFoldDB; A0A3Q0CLU8; -.
DR STRING; 10036.ENSMAUP00000010261; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 5.
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 PANTHER; PTHR24253:SF159; PROSTASIN; 1.
DR PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR Pfam; PF00089; Trypsin; 4.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 4.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1243
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018108544"
FT DOMAIN 47..291
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 326..560
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 606..813
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 946..1187
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 20..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1243 AA; 134126 MW; 6E80E61198119C7C CRC64;
MSQHLFLPVV MMVVSPIPGT SQDSAISPTQ GESEDLDCGH PEPSSRIVGG SDARPGTWPW
QVSLHHGGGH ICGGSLIAPS WVLSAAHCFV TNETLEPADE WSVLLGVHSQ DGPMDGAHLR
SVAAILVPDN YSRVELGSDV ALLRLASPAR LSPSVRPVCL PRASHRFAHG TACWATGWGD
VQEADPLPLP WVLQEVELRL LGEAACQCLY SRPGPFNLTF QLLPGMLCAG YPEGRRDTCQ
GDSGGPLVCE DGGRWFQAGI TSFGFGCGRR NRPGVFTAVA PYESWIREQV MGSEPGPAFP
SQLHKPQSGP QEPREENCTF AQPECGKASR PGIWPWEAQV MVPGSRPCYG VLVSDSWVLA
PASCSLDYPI QQPRTSDSPP RDLEAWRVLL PSRPEGERVA RLVPHENASK DSASDLALLQ
LRTRVNLTAA PSAVCLPHPE HFFLPGSRCR LARWGRGEPA PGSSAQLEAQ LMNSWWCHCL
YGRQGASVPP PGDPPHLLCP AYLEEEEAGQ CWKDAGWSLL CREEGTWFLA GHRTLSNGCL
RPRAFSPLQT HGPWISHVTQ GAYLEDQLTW DWGPEGEETE KQICPPHTEH GACGLRPKAT
PAGALWPWLT EVHVTGNRVC TGILVAPGWV LAATHCILRL GSTTVPYIEV YLGQAGARSL
PQGHQVSRSV ISIRLPRHLG LRPPLALLEL NSQVEPSPSA LPICLQPGGI PPGASCWVLG
WKDPQDRVPV AAAVTILTPR LCHCLYQGIL TPGTFCVLYT EGQEDKCEVT SAPPLLCQTE
GGPWVLMGMA VRGSQELFAA IGPEAAWISQ TVGEAHFLPP SGSPYWPPED SDLCHQDLAG
AASSPRAAAL LLLPLAPLIQ GILGFLLPSR HPDPAFKASL PFLPFLPRVS RPPARELSTW
AMALMVGRGP GQREAVAILL LMGLLQPRTG AAGAEASCGV VMQPRITGGS SAKPGQWPWQ
VSITYDGIHV CGGSLVSDQW VVSAAHCFPR EHYRDQYEVK LGAHQLDSYS NDTVVRTVAR
IISHSSYREE GSQGDIALVH LSSPVNFSRH IKPICLPAAN ASFPNGLHCT VTGWGHVAPS
VSLQTPKPLQ QLEVPLISRE TCSCLYNINA VPEEPHTIQP DMLCAGYVEG GKDACQGDSG
GPLSCPIEGL WYLAGIVSWG DACGAPNRPG VYTLTSTYAS WIHHNVAELQ PRMVPQTQES
QPDGHLCNHH HVFNSAAAQG LLRPLPFLPL GLTLGLFCLW FEH
//