CREL1_MOUSE
ID CREL1_MOUSE Reviewed; 420 AA.
AC Q91XD7; Q8BGJ8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=12137942; DOI=10.1016/s0378-1119(02)00696-0;
RA Rupp P.A., Fouad G.T., Egelston C.A., Reifsteck C.A., Olson S.B.,
RA Knosp W.M., Glanville R.W., Thornburg K.L., Robinson S.W., Maslen C.L.;
RT "Identification, genomic organization and mRNA expression of CRELD1, the
RT founding member of a unique family of matricellular proteins.";
RL Gene 293:47-57(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, Liver, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30407909; DOI=10.7554/elife.39649;
RA D'Alessandro M., Richard M., Stigloher C., Gache V., Boulin T.,
RA Richmond J.E., Bessereau J.L.;
RT "CRELD1 is an evolutionarily-conserved maturational enhancer of ionotropic
RT acetylcholine receptors.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Protein disulfide isomerase (By similarity). Promotes the
CC localization of acetylcholine receptors (AChRs) to the plasma membrane
CC (PubMed:30407909). {ECO:0000250|UniProtKB:Q9CYA0,
CC ECO:0000269|PubMed:30407909}.
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 -!- TISSUE SPECIFICITY: Expressed in myoblast C2C12 cells (at protein
CC level). {ECO:0000269|PubMed:30407909}.
CC -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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DR EMBL; AK050160; BAC34101.1; -; mRNA.
DR EMBL; AK050455; BAC34266.1; -; mRNA.
DR EMBL; AK155777; BAE33433.1; -; mRNA.
DR EMBL; BC010804; AAH10804.1; -; mRNA.
DR EMBL; BC023893; AAH23893.1; -; mRNA.
DR EMBL; BC025932; AAH25932.1; -; mRNA.
DR EMBL; BC029065; AAH29065.1; -; mRNA.
DR CCDS; CCDS20423.1; -.
DR RefSeq; NP_598691.1; NM_133930.2.
DR AlphaFoldDB; Q91XD7; -.
DR STRING; 10090.ENSMUSP00000032422; -.
DR GlyConnect; 2247; 2 N-Linked glycans (1 site).
DR GlyGen; Q91XD7; 1 site, 2 N-linked glycans (1 site).
DR PhosphoSitePlus; Q91XD7; -.
DR jPOST; Q91XD7; -.
DR MaxQB; Q91XD7; -.
DR PaxDb; Q91XD7; -.
DR PRIDE; Q91XD7; -.
DR ProteomicsDB; 284123; -.
DR Antibodypedia; 25846; 127 antibodies from 24 providers.
DR DNASU; 171508; -.
DR Ensembl; ENSMUST00000032422; ENSMUSP00000032422; ENSMUSG00000030284.
DR GeneID; 171508; -.
DR KEGG; mmu:171508; -.
DR UCSC; uc009dgo.1; mouse.
DR CTD; 78987; -.
DR MGI; MGI:2152539; Creld1.
DR VEuPathDB; HostDB:ENSMUSG00000030284; -.
DR eggNOG; KOG4260; Eukaryota.
DR GeneTree; ENSGT00940000160255; -.
DR HOGENOM; CLU_038974_1_1_1; -.
DR InParanoid; Q91XD7; -.
DR OMA; EWLCIEQ; -.
DR OrthoDB; 883628at2759; -.
DR PhylomeDB; Q91XD7; -.
DR TreeFam; TF316507; -.
DR BioGRID-ORCS; 171508; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Creld1; mouse.
DR PRO; PR:Q91XD7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91XD7; protein.
DR Bgee; ENSMUSG00000030284; Expressed in urinary bladder urothelium and 226 other tissues.
DR ExpressionAtlas; Q91XD7; baseline and differential.
DR Genevisible; Q91XD7; MM.
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; 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 1: Evidence at protein 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_0000042782"
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; 45718 MW; 4066BF2D739D3179 CRC64;
MAPLPPRGLV PSLLWCLSLF LSLPGPVWLQ PSPPPHPSPR AEPHPCHTCR ALVDNFNKGL
ERTIRDNFGG GNTAWEEEKL SKYKDSETRL VEVLEGVCSR SDFECHRLLE LSEELVENWW
FHRQQEAPDL FQWLCSDSLK LCCPSGTFGP SCLPCPGGTE RPCGGYGQCE GEGTRGGSGH
CDCQAGYGGE ACGQCGLGYF EAERNSSHLV CSACFGPCAR CTGPEESHCL QCKKGWALHH
LKCVDIDECG TEQATCGADQ FCVNTEGSYE CRDCAKACLG CMGAGPGRCK KCSRGYQQVG
SKCLDVDECE TVVCPGENEK CENTEGGYRC VCAEGYRQED GICVKEQVPE SAGFFAEMTE
DEMVVLQQMF FGVIICALAT LAAKGDLVFT AIFIGAVAAM TGYWLSERSD RVLEGFIKGR
