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Q91XD7 (CREL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine-rich with EGF-like domain protein 1
Gene names
Name:Creld1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the CRELD family.

Contains 2 EGF-like domains.

Contains 2 FU (furin-like) repeats.

Ontologies

Keywords
   Cellular componentMembrane
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 420391Cysteine-rich with EGF-like domain protein 1
PRO_0000042782

Regions

Topological domain30 – 362333Extracellular Potential
Transmembrane363 – 38321Helical; Potential
Topological domain3841Cytoplasmic Potential
Transmembrane385 – 40521Helical; Potential
Topological domain406 – 42015Extracellular Potential
Domain153 – 19341EGF-like 1
Repeat208 – 25548FU 1
Repeat268 – 31548FU 2
Domain305 – 34238EGF-like 2; calcium-binding Potential

Amino acid modifications

Glycosylation2051N-linked (GlcNAc...) Potential
Disulfide bond155 ↔ 169 By similarity
Disulfide bond163 ↔ 181 By similarity
Disulfide bond183 ↔ 192 By similarity
Disulfide bond309 ↔ 321 By similarity
Disulfide bond314 ↔ 330 By similarity
Disulfide bond332 ↔ 343 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91XD7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 4066BF2D739D3179

FASTA42045,718
        10         20         30         40         50         60 
MAPLPPRGLV PSLLWCLSLF LSLPGPVWLQ PSPPPHPSPR AEPHPCHTCR ALVDNFNKGL 

        70         80         90        100        110        120 
ERTIRDNFGG GNTAWEEEKL SKYKDSETRL VEVLEGVCSR SDFECHRLLE LSEELVENWW 

       130        140        150        160        170        180 
FHRQQEAPDL FQWLCSDSLK LCCPSGTFGP SCLPCPGGTE RPCGGYGQCE GEGTRGGSGH 

       190        200        210        220        230        240 
CDCQAGYGGE ACGQCGLGYF EAERNSSHLV CSACFGPCAR CTGPEESHCL QCKKGWALHH 

       250        260        270        280        290        300 
LKCVDIDECG TEQATCGADQ FCVNTEGSYE CRDCAKACLG CMGAGPGRCK KCSRGYQQVG 

       310        320        330        340        350        360 
SKCLDVDECE TVVCPGENEK CENTEGGYRC VCAEGYRQED GICVKEQVPE SAGFFAEMTE 

       370        380        390        400        410        420 
DEMVVLQQMF FGVIICALAT LAAKGDLVFT AIFIGAVAAM TGYWLSERSD RVLEGFIKGR 

« Hide

References

« Hide 'large scale' references
[1]"Identification, genomic organization and mRNA expression of CRELD1, the founding member of a unique family of matricellular proteins."
Rupp P.A., Fouad G.T., Egelston C.A., Reifsteck C.A., Olson S.B., Knosp W.M., Glanville R.W., Thornburg K.L., Robinson S.W., Maslen C.L.
Gene 293:47-57(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney, Liver and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK050160 mRNA. Translation: BAC34101.1.
AK050455 mRNA. Translation: BAC34266.1.
AK155777 mRNA. Translation: BAE33433.1.
BC010804 mRNA. Translation: AAH10804.1.
BC023893 mRNA. Translation: AAH23893.1.
BC025932 mRNA. Translation: AAH25932.1.
BC029065 mRNA. Translation: AAH29065.1.
RefSeqNP_598691.1. NM_133930.1.
UniGeneMm.41593.

3D structure databases

ProteinModelPortalQ91XD7.
SMRQ91XD7. Positions 138-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91XD7. 2 interactions.
MINTMINT-4997877.
STRING10090.ENSMUSP00000032422.

Proteomic databases

PaxDbQ91XD7.
PRIDEQ91XD7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032422; ENSMUSP00000032422; ENSMUSG00000030284.
GeneID171508.
KEGGmmu:171508.
UCSCuc009dgo.1. mouse.

Organism-specific databases

CTD78987.
MGIMGI:2152539. Creld1.

Phylogenomic databases

eggNOGNOG315654.
GeneTreeENSGT00680000100014.
HOGENOMHOG000004778.
HOVERGENHBG081344.
InParanoidQ91XD7.
OMAEPHPCHT.
OrthoDBEOG7Z3F4B.
PhylomeDBQ91XD7.
TreeFamTF316507.

Gene expression databases

BgeeQ91XD7.
CleanExMM_CRELD1.
GenevestigatorQ91XD7.

Family and domain databases

InterProIPR021852. DUF3456.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR002049. EGF_laminin.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamPF11938. DUF3456. 2 hits.
PF07645. EGF_CA. 2 hits.
[Graphical view]
SMARTSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00261. FU. 2 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio371024.
PROQ91XD7.
SOURCESearch...

Entry information

Entry nameCREL1_MOUSE
AccessionPrimary (citable) accession number: Q91XD7
Secondary accession number(s): Q8BGJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot