CREL2_RAT
ID CREL2_RAT Reviewed; 349 AA.
AC Q4G063;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16238698; DOI=10.1111/j.1471-4159.2005.03473.x;
RA Ortiz J.A., Castillo M., Dominguez del Toro E., Mulet J., Gerber S.,
RA Valor L.M., Sala S., Sala F., Gutierrez L.M., Criado M.;
RT "The cysteine-rich with EGF-like domains 2 (CRELD2) protein interacts with
RT the large cytoplasmic domain of human neuronal nicotinic acetylcholine
RT receptor alpha4 and beta2 subunits.";
RL J. Neurochem. 95:1585-1596(2005).
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 -!- TISSUE SPECIFICITY: Broadly expressed in brain (at protein level).
CC {ECO:0000269|PubMed:16238698}.
CC -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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DR EMBL; BC098722; AAH98722.1; -; mRNA.
DR RefSeq; NP_001032285.1; NM_001037208.1.
DR AlphaFoldDB; Q4G063; -.
DR STRING; 10116.ENSRNOP00000006357; -.
DR GlyGen; Q4G063; 2 sites.
DR iPTMnet; Q4G063; -.
DR PhosphoSitePlus; Q4G063; -.
DR PaxDb; Q4G063; -.
DR PRIDE; Q4G063; -.
DR Ensembl; ENSRNOT00000006357; ENSRNOP00000006357; ENSRNOG00000004659.
DR GeneID; 362978; -.
DR KEGG; rno:362978; -.
DR CTD; 79174; -.
DR RGD; 1310614; Creld2.
DR eggNOG; KOG4260; Eukaryota.
DR GeneTree; ENSGT00940000160071; -.
DR HOGENOM; CLU_038974_1_0_1; -.
DR InParanoid; Q4G063; -.
DR OMA; DQEACVD; -.
DR OrthoDB; 883628at2759; -.
DR PhylomeDB; Q4G063; -.
DR TreeFam; TF316507; -.
DR PRO; PR:Q4G063; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004659; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q4G063; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
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; 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 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Endoplasmic reticulum;
KW Glycoprotein; Isomerase; Redox-active center; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..349
FT /note="Protein disulfide isomerase Creld2"
FT /id="PRO_0000256247"
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 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 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 349 AA; 38251 MW; 5E8ABE53CB9F8850 CRC64;
MHLLLAAGFG LLLLLLPPPA ASKKPTQCQR CRTLVDKFNQ GMANTARKNF GGGNTAWEEK
TLSKYEFSEI RLLEIMEGLC DSSDFECNQL LEQQEEQLEA WWQSLKKDYP NLFEWFCVRT
LKACCLPGTY GPDCKECQGG SERPCSGNGY CSGDGSRQGD GSCQCHAGYK GPLCIDCMDG
YFSLQRNETH SICLACDESC KTCSGPSNKD CVQCEVGWAR VEDACVDVDE CAAETPPCSE
AQYCENVNGS YICEECDSTC VGCTGKGPAN CKECIAGYTK QSGQCADIDE CSLEEKACKR
RNENCYNVPG SFVCVCPDGF EETEDACVQT AQSEVTEENP TQPLSHEDL
