CREL1_RAT
ID CREL1_RAT Reviewed; 420 AA.
AC Q4V7F2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein disulfide isomerase Creld1 {ECO:0000305};
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:Q9CYA0};
DE AltName: Full=Cysteine-rich with EGF-like domain protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=Creld1;
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=Placenta;
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).
CC -!- FUNCTION: Protein disulfide isomerase (By similarity). Promotes the
CC localization of acetylcholine receptors (AChRs) to the plasma membrane
CC (By similarity). {ECO:0000250|UniProtKB:Q91XD7,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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DR EMBL; BC097951; AAH97951.1; -; mRNA.
DR RefSeq; NP_001019954.1; NM_001024783.1.
DR AlphaFoldDB; Q4V7F2; -.
DR STRING; 10116.ENSRNOP00000013052; -.
DR GlyGen; Q4V7F2; 1 site.
DR jPOST; Q4V7F2; -.
DR PaxDb; Q4V7F2; -.
DR PRIDE; Q4V7F2; -.
DR Ensembl; ENSRNOT00000013052; ENSRNOP00000013052; ENSRNOG00000009414.
DR GeneID; 312638; -.
DR KEGG; rno:312638; -.
DR UCSC; RGD:1309412; rat.
DR CTD; 78987; -.
DR RGD; 1309412; Creld1.
DR eggNOG; KOG4260; Eukaryota.
DR GeneTree; ENSGT00940000160255; -.
DR HOGENOM; CLU_038974_1_1_1; -.
DR InParanoid; Q4V7F2; -.
DR OMA; EWLCIEQ; -.
DR OrthoDB; 883628at2759; -.
DR PhylomeDB; Q4V7F2; -.
DR TreeFam; TF316507; -.
DR PRO; PR:Q4V7F2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009414; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q4V7F2; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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 Pfam; PF11938; DUF3456; 1.
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; Glycoprotein; Isomerase;
KW Membrane; Redox-active center; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..420
FT /note="Protein disulfide isomerase Creld1"
FT /id="PRO_0000042783"
FT TOPO_DOM 30..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 153..193
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 208..255
FT /note="FU 1"
FT REPEAT 268..315
FT /note="FU 2"
FT DOMAIN 305..342
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MOTIF 46..49
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:Q19267"
FT MOTIF 278..281
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..49
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT DISULFID 155..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 163..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 278..281
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT DISULFID 309..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 314..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 332..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 420 AA; 45697 MW; 5E424A5C21E7AAB8 CRC64;
MAPQPLRGLV PFLLWCLSLF LSLPGPVWLQ PSPPPHSAPR AEPHPCHTCR ALVDSFNKGL
ERTIRDNFGG GNTAWEEEKL SKYKDSETRL VEVLEGVCSK SDFECHRLLE LSEELVEAWW
FHRQQEAPDL FQWLCSDSLK LCCPSGTFGP SCLPCPGGTE RPCGGYGQCE GEGTRGGSGH
CDCQAGYGGE ACGQCGLGYF EAERNSSHLV CSACFGPCAR CTGPEESHCL QCRKGWALHH
LKCVDIDECG TEQATCGAAQ FCVNTEGSYE CRDCAKACLG CMGAGPGRCK KCSRGYQQVG
SKCLDVDECE TVVCPGENEQ CENTEGSYRC VCAEGFRQED GICVKEQIPE SAGFFAEMTE
DEMVVLQQMF FGVIICALAT LAAKGDLVFT AIFIGAVAAM TGYWLSERSD RVLEGFIKGR
