ID   CREL2_CRIGR             Reviewed;         348 AA.
AC   Q60438;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Protein disulfide isomerase CRELD2 {ECO:0000305};
DE            EC=5.3.4.1 {ECO:0000250|UniProtKB:Q9CYA0};
DE   AltName: Full=Cysteine-rich with EGF-like domain protein 2 {ECO:0000305};
DE   AltName: Full=Protein HT;
DE   Flags: Precursor;
GN   Name=CRELD2;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen H., Okubo T., Ling V., Zhang W.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein disulfide isomerase (By similarity). Might play a
CC       role in the unfolded protein response (By similarity). May regulate
CC       transport of alpha4-beta2 neuronal acetylcholine receptor (By
CC       similarity). {ECO:0000250|UniProtKB:Q6UXH1,
CC       ECO:0000250|UniProtKB:Q9CYA0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:Q9CYA0};
CC   -!- SUBUNIT: Interacts with CHRNA4 (By similarity). Component of a complex
CC       containing at least CRELD2, MANF, MATN3 and PDIA4 (By similarity).
CC       {ECO:0000250|UniProtKB:Q6UXH1, ECO:0000250|UniProtKB:Q9CYA0}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q6UXH1}.
CC   -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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DR   EMBL; U48852; AAA91469.1; -; mRNA.
DR   RefSeq; NP_001231065.1; NM_001244136.1.
DR   AlphaFoldDB; Q60438; -.
DR   STRING; 10029.NP_001231065.1; -.
DR   GeneID; 100689097; -.
DR   KEGG; cge:100689097; -.
DR   CTD; 79174; -.
DR   eggNOG; KOG4260; Eukaryota.
DR   OrthoDB; 883628at2759; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   CDD; cd00064; FU; 2.
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   Pfam; PF07645; EGF_CA; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00261; FU; 2.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; EGF-like domain; Endoplasmic reticulum;
KW   Glycoprotein; Isomerase; Redox-active center; Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..348
FT                   /note="Protein disulfide isomerase CRELD2"
FT                   /id="PRO_0000256245"
FT   DOMAIN          135..177
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          192..239
FT                   /note="FU 1"
FT   REPEAT          252..299
FT                   /note="FU 2"
FT   DOMAIN          289..329
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   MOTIF           30..33
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT   MOTIF           262..265
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..33
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT   DISULFID        139..153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        147..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        167..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        262..265
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT   DISULFID        293..307
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        300..316
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        318..328
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   348 AA;  38199 MW;  BD61F6C89971BB6D CRC64;
     MHLPPAAAVG LLLLLLPPPA RVASRKPTMC QRCRALVDKF NQGMANTARK NFGGGNTAWE
     EKSLSKYEFS EIRLLEIMEG LCDSNDFECN QLLEQHEEQL EAWWQTLKKE CPNLFEWFCV
     HTLKACCLPG TYGPDCQECQ GGSQRPCSGN GHCDGDGSRQ GDGSCQCHVG YKGPLCIDCM
     DGYFSLLRNE THSFCTACDE SCKTCSGPTN KGCVECEVGW TRVEDACVDV DECAAETPPC
     SNVQYCENVN GSYTCEECDS TCVGCTGKGP ANCKECISGY SKQKGECADI DECSLETKVC
     KKENENCYNT PGSFVCVCPE GFEEDRRCLC TDSRRRSGRG KSHTATLP