GenomeNet

Database: UniProt
Entry: Q91XD7
LinkDB: Q91XD7
Original site: Q91XD7 
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   13-FEB-2019, entry version 134.
DE   RecName: Full=Cysteine-rich with EGF-like domain protein 1;
DE   Flags: Precursor;
GN   Name=Creld1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Maslen C.L.;
RT   "Identification, genomic organization and mRNA expression of CRELD1,
RT   the 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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   UniGene; Mm.41593; -.
DR   ProteinModelPortal; Q91XD7; -.
DR   SMR; Q91XD7; -.
DR   IntAct; Q91XD7; 2.
DR   MINT; Q91XD7; -.
DR   STRING; 10090.ENSMUSP00000032422; -.
DR   PhosphoSitePlus; Q91XD7; -.
DR   jPOST; Q91XD7; -.
DR   MaxQB; Q91XD7; -.
DR   PaxDb; Q91XD7; -.
DR   PRIDE; Q91XD7; -.
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   eggNOG; KOG4260; Eukaryota.
DR   eggNOG; ENOG41107X2; LUCA.
DR   GeneTree; ENSGT00940000160255; -.
DR   HOGENOM; HOG000004778; -.
DR   HOVERGEN; HBG081344; -.
DR   InParanoid; Q91XD7; -.
DR   OMA; FHRQQEA; -.
DR   OrthoDB; 883628at2759; -.
DR   PhylomeDB; Q91XD7; -.
DR   TreeFam; TF316507; -.
DR   PRO; PR:Q91XD7; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000030284; Expressed in 252 organ(s), highest expression level in dorsal root ganglion.
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:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   CDD; cd00064; FU; 1.
DR   InterPro; IPR021852; DUF3456.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; Laminin_EGF.
DR   Pfam; PF11938; DUF3456; 1.
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; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       {ECO:0000255}.
FT   CHAIN        30    420       Cysteine-rich with EGF-like domain
FT                                protein 1.
FT                                /FTId=PRO_0000042782.
FT   TOPO_DOM     30    362       Extracellular. {ECO:0000255}.
FT   TRANSMEM    363    383       Helical. {ECO:0000255}.
FT   TOPO_DOM    384    384       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    385    405       Helical. {ECO:0000255}.
FT   TOPO_DOM    406    420       Extracellular. {ECO:0000255}.
FT   DOMAIN      153    193       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      208    255       FU 1.
FT   REPEAT      268    315       FU 2.
FT   DOMAIN      305    342       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CARBOHYD    205    205       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    155    169       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    163    181       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    183    192       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    309    321       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    314    330       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    332    343       {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
//
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