CREL1_BOVIN
ID CREL1_BOVIN Reviewed; 420 AA.
AC Q5EA46; Q58CS1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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;
DE Flags: Precursor;
GN Name=CRELD1;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46723.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT020723; AAX08740.1; -; mRNA.
DR EMBL; BT021876; AAX46723.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001014851.3; NM_001014851.3.
DR AlphaFoldDB; Q5EA46; -.
DR STRING; 9913.ENSBTAP00000014377; -.
DR PaxDb; Q5EA46; -.
DR GeneID; 504854; -.
DR KEGG; bta:504854; -.
DR CTD; 78987; -.
DR eggNOG; KOG4260; Eukaryota.
DR InParanoid; Q5EA46; -.
DR OrthoDB; 883628at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; 2.
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_0000042780"
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..344
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"
FT CONFLICT 346
FT /note="D -> E (in Ref. 1; AAX46723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 45368 MW; D6332A491CF08B91 CRC64;
MAPRSSRGIA PAMLCGLSLF LGFPGLVWVQ ISVPPQSSPH TEPHPCHTCR GLVDSFNKGL
ERTIRDNFGG GNTAWEEEKL SKYKDSETRL VEVLEGVCSK SDFECHRLLE LSEELVESWW
FHKQQEAPDL FQWLCSDSLK LCCPSGTFGP SCLPCPGGAE RPCGGYGHCE GEGTRGGSGH
CDCQAGYGGE ACGQCGLGYF EAERNASHLV CSACFGPCAR CSGPEESHCL QCKKGWALHH
LKCVDIDECG TERASCGADQ FCVNTEGSYE CRDCAKACLG CMGAGPGRCK KCSPGYQQVG
SKCLDVDECE TAVCPGENQQ CENTEGSYRC ICADGYKQME GICVKDQIPE SAGFFSEMTE
DELVVLQQMF FGVIICALAT LAAKGDLVFT AIFIGAVAAM TGYWLSERSD RVLEGFIKGR
