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Protein

Cartilage acidic protein 1

Gene

Crtac1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • axonal fasciculation Source: MGI
  • negative regulation of receptor binding Source: MGI
  • olfactory bulb development Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Cartilage acidic protein 1
Alternative name(s):
68 kDa chondrocyte-expressed protein
Short name:
CEP-68
ASPIC
Protein CRTAC1-B
Gene namesi
Name:Crtac1
Synonyms:Aspic1, Cep68
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1920082. Crtac1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • growth cone Source: MGI
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 646618Cartilage acidic protein 1PRO_0000007498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi564 ↔ 578Sequence analysis
Disulfide bondi571 ↔ 587Sequence analysis
Disulfide bondi593 ↔ 606Sequence analysis

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ8R555.
PaxDbiQ8R555.
PeptideAtlasiQ8R555.
PRIDEiQ8R555.

PTM databases

iPTMnetiQ8R555.
PhosphoSiteiQ8R555.

Expressioni

Gene expression databases

BgeeiQ8R555.
CleanExiMM_CEP68.
MM_CRTAC1.
GenevisibleiQ8R555. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8R555. 1 interaction.
STRINGi10090.ENSMUSP00000044858.

Structurei

3D structure databases

ProteinModelPortaliQ8R555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati47 – 8943FG-GAP 1; atypicalAdd
BLAST
Repeati106 – 14843FG-GAP 2; atypicalAdd
BLAST
Repeati284 – 33451FG-GAP 3; atypicalAdd
BLAST
Repeati396 – 43843FG-GAP 4; atypicalAdd
BLAST
Domaini560 – 60647EGF-likeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi623 – 64018Ala-richAdd
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.Curated
Contains 4 FG-GAP repeats.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IHAW. Eukaryota.
ENOG410ZVH2. LUCA.
GeneTreeiENSGT00390000013726.
HOGENOMiHOG000230473.
HOVERGENiHBG051111.
InParanoidiQ8R555.
OMAiNNNWLRV.
OrthoDBiEOG76QFGR.
PhylomeDBiQ8R555.
TreeFamiTF333171.

Family and domain databases

InterProiIPR027039. Crtac1.
IPR001881. EGF-like_Ca-bd_dom.
IPR018097. EGF_Ca-bd_CS.
IPR011519. UnbV_ASPIC.
[Graphical view]
PANTHERiPTHR16026. PTHR16026. 1 hit.
PfamiPF07645. EGF_CA. 1 hit.
PF07593. UnbV_ASPIC. 1 hit.
[Graphical view]
SMARTiSM00179. EGF_CA. 1 hit.
[Graphical view]
PROSITEiPS01187. EGF_CA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8R555-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSADPGMV RMALLLLPPL WLLPLTGGSQ RAEPMFTAVT NSVLPPDYDS
60 70 80 90 100
NPTQLNYGVA VTDVDHDGDF EIVVAGYTGP NLVLKYNRAQ NRLVNIAVDE
110 120 130 140 150
RSSPYYALRD RQGNAIGVTA CDIDGDGREE IYFLNTNNAF SGVATYTDKL
160 170 180 190 200
FKFRNNRWED ILSDDVNVAR GVASLFAGRS VACVDRTGSG RYSIYIANYA
210 220 230 240 250
YGDVGPDALI EMDPEASDLS RGILALRDVA AEAGVSKYTA GRGVSVGPIL
260 270 280 290 300
SSSASDIFCD NENGPNFLFH NQGNGTFVDT AASAGVDDPH QHGRGVALAD
310 320 330 340 350
FNRDGKVDIV YGNWNGPHRL YLQMSAHGKV RFRDIASPKF STPSPVRTVI
360 370 380 390 400
AADFDNDQEL EVFFNNIAYR SSSANRLFRV IRREHGDPLI EELNPGDALE
410 420 430 440 450
PEGRGTGGVV TDFDGDGMLD LILSHGESMA QPLSVFRGNQ GFSNNWLRVV
460 470 480 490 500
PRTRFGAFAR GAKVVLYTKK SGAHLRIIDG GSGYLCEMEP VAHFGLGRDE
510 520 530 540 550
ASSVEVTWPD GKMVSRSVAS EEMNSVLEIL YPQDEDKLQN TAPLECGQGF
560 570 580 590 600
SQQDNGHCMD TNECIQFPFV CPRDKPVCVN TYGSYRCRTN KRCNRGYEPN
610 620 630 640
EDGTACVAQV AFLGGYSSAA FRLSEPLSQA SYLSLGLGLC LQLYAL
Length:646
Mass (Da):70,325
Last modified:June 1, 2002 - v1
Checksum:i154C45E636DF2D98
GO

Sequence cautioni

The sequence AAH24472.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911R → G in BAC27817 (PubMed:16141072).Curated
Sequence conflicti331 – 3311R → Q in BAC27817 (PubMed:16141072).Curated
Sequence conflicti471 – 4711S → C in BAE28721 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ421516 mRNA. Translation: CAD13395.1.
AK149020 mRNA. Translation: BAE28721.1.
AK032328 mRNA. Translation: BAC27817.1.
AK049801 mRNA. Translation: BAC33924.1.
AK149069 mRNA. Translation: BAE28729.1.
BC024472 mRNA. Translation: AAH24472.1. Different initiation.
CCDSiCCDS29828.1.
RefSeqiNP_660105.3. NM_145123.4.
UniGeneiMm.313558.

Genome annotation databases

EnsembliENSMUST00000048630; ENSMUSP00000044858; ENSMUSG00000042401.
GeneIDi72832.
KEGGimmu:72832.
UCSCiuc008hno.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ421516 mRNA. Translation: CAD13395.1.
AK149020 mRNA. Translation: BAE28721.1.
AK032328 mRNA. Translation: BAC27817.1.
AK049801 mRNA. Translation: BAC33924.1.
AK149069 mRNA. Translation: BAE28729.1.
BC024472 mRNA. Translation: AAH24472.1. Different initiation.
CCDSiCCDS29828.1.
RefSeqiNP_660105.3. NM_145123.4.
UniGeneiMm.313558.

3D structure databases

ProteinModelPortaliQ8R555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R555. 1 interaction.
STRINGi10090.ENSMUSP00000044858.

PTM databases

iPTMnetiQ8R555.
PhosphoSiteiQ8R555.

Proteomic databases

MaxQBiQ8R555.
PaxDbiQ8R555.
PeptideAtlasiQ8R555.
PRIDEiQ8R555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048630; ENSMUSP00000044858; ENSMUSG00000042401.
GeneIDi72832.
KEGGimmu:72832.
UCSCiuc008hno.1. mouse.

Organism-specific databases

CTDi55118.
MGIiMGI:1920082. Crtac1.

Phylogenomic databases

eggNOGiENOG410IHAW. Eukaryota.
ENOG410ZVH2. LUCA.
GeneTreeiENSGT00390000013726.
HOGENOMiHOG000230473.
HOVERGENiHBG051111.
InParanoidiQ8R555.
OMAiNNNWLRV.
OrthoDBiEOG76QFGR.
PhylomeDBiQ8R555.
TreeFamiTF333171.

Miscellaneous databases

PROiQ8R555.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R555.
CleanExiMM_CEP68.
MM_CRTAC1.
GenevisibleiQ8R555. MM.

Family and domain databases

InterProiIPR027039. Crtac1.
IPR001881. EGF-like_Ca-bd_dom.
IPR018097. EGF_Ca-bd_CS.
IPR011519. UnbV_ASPIC.
[Graphical view]
PANTHERiPTHR16026. PTHR16026. 1 hit.
PfamiPF07645. EGF_CA. 1 hit.
PF07593. UnbV_ASPIC. 1 hit.
[Graphical view]
SMARTiSM00179. EGF_CA. 1 hit.
[Graphical view]
PROSITEiPS01187. EGF_CA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel form of CRTAC1 expressed in human and mouse brain generated by alternative splicing of a newly identified last exon."
    Steck E., Richter W.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  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.
    , 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.
    Tissue: Olfactory bulb, Spinal cord and Sympathetic ganglion.
  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] OF 143-646.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiCRAC1_MOUSE
AccessioniPrimary (citable) accession number: Q8R555
Secondary accession number(s): Q3UF32
, Q3UF40, Q8BMF1, Q8R3V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.