ID A0A1U7RGI3_MESAU Unreviewed; 356 AA.
AC A0A1U7RGI3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN Name=LOC101830943 {ECO:0000313|RefSeq:XP_005088252.2};
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_005088252.2};
RN [1] {ECO:0000313|RefSeq:XP_005088252.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_005088252.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182};
CC -!- SIMILARITY: Belongs to the CRELD family.
CC {ECO:0000256|ARBA:ARBA00005897}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_005088252.2; XM_005088195.3.
DR AlphaFoldDB; A0A1U7RGI3; -.
DR eggNOG; KOG4260; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.90.20.10; Plasmodium vivax P25 domain; 1.
DR InterPro; IPR021852; DUF3456.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24038:SF13; PROTEIN DISULFIDE-ISOMERASE; 1.
DR PANTHER; PTHR24038; STABILIN; 1.
DR Pfam; PF11938; DUF3456; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00261; FU; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS01248; EGF_LAM_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..356
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018124983"
FT DOMAIN 153..193
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 305..342
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 183..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 356
FT /evidence="ECO:0000313|RefSeq:XP_005088252.2"
SQ SEQUENCE 356 AA; 38609 MW; CED37A1317B5EA11 CRC64;
MAPQPLRGLV PSLLWSLSLF LSLPGPVWLQ PSPAPHSSPR VEPHPCHTCR ALVDSFNKGL
ERTIRDNFGG GNTAWEEEKL SKYKDSETRL VEVLEGVCSK SDFECHRLLE LSEELVETWW
FHRQQEAPDL SQWLCSDSLK LCCPSGTFGP SCLPCPGGTE RPCGGYGQCE GEGTRGGSGH
CDCQVGYGGE ACGQCGLGYF EAERNSSHLV CSACFGPCAR CTGPEESHCL QCKKGWALHH
LKCVDIDECG TEQATCGADQ FCVNTEGSYE CRDCAKACLG CMGAGPGRCK KCSCGYQQVG
SKCLDVDECE TVVCPGENEQ CENTEGSYRC VCAEGYRQEE GVCMKEKIPE PAGIFA
//
