ID   CREL2_BOVIN             Reviewed;         351 AA.
AC   Q2KIT5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Flags: Precursor;
GN   Name=CRELD2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) 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; BC112517; AAI12518.1; -; mRNA.
DR   RefSeq; NP_001039656.1; NM_001046191.1.
DR   AlphaFoldDB; Q2KIT5; -.
DR   STRING; 9913.ENSBTAP00000054551; -.
DR   PaxDb; Q2KIT5; -.
DR   PRIDE; Q2KIT5; -.
DR   GeneID; 515222; -.
DR   KEGG; bta:515222; -.
DR   CTD; 79174; -.
DR   eggNOG; KOG4260; Eukaryota.
DR   HOGENOM; CLU_038974_1_0_1; -.
DR   InParanoid; Q2KIT5; -.
DR   OrthoDB; 883628at2759; -.
DR   TreeFam; TF316507; -.
DR   Proteomes; UP000009136; Unplaced.
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; 1.
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; 2.
DR   SMART; SM00181; EGF; 4.
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; Reference proteome; Repeat;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..351
FT                   /note="Protein disulfide isomerase CRELD2"
FT                   /id="PRO_0000256243"
FT   DOMAIN          133..175
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          190..237
FT                   /note="FU 1"
FT   REPEAT          250..297
FT                   /note="FU 2"
FT   DOMAIN          287..328
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          329..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           28..31
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT   MOTIF           260..263
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..31
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT   DISULFID        137..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        145..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        165..174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        260..263
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT   DISULFID        291..305
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        298..314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        316..327
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   351 AA;  38230 MW;  C11552BC0BE06012 CRC64;
     MRPPAPAVLG LLLLLLPTGE ATKKPTPCKR CRELVDKFNQ GMVDTAKKNF GGGNTAWEEK
     TLSKYEFSEV RLLEIVEGLC EASDFECNQL LEEQEELLEA WWLRLKKKHP DLFEWFCVQT
     LKACCSPGTY GPDCLACQGG SERPCSGNGH CVGDGTREGD GSCQCHLGYQ GPLCSDCMDG
     YFRSPTSETH SICSACDEAC KTCVGPTNRD CGQCEVGWVR QDDACVDVDE CAAEPPPCED
     TQYCENVNGS FVCEECDPTC MGCTGKGPTQ CRECIAGYSK ESGQCEDIDE CSLAEKPCLR
     DNENCYNTPG SFVCVCPDGF EEAEDTCVQT RPAGAEATEA SPTQPPSRED L