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Protein

Chondroitin proteoglycan 1

Gene

cpg-1

Organism
Caenorhabditis briggsae
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Required for polar body extrusion during cytokinesis in embryo development. Affects cortical granule size. Shown to have roles in meiotic chromosome segregation, osmotic barrier function and polarization in conjunction with cpg-2. Binds chitin (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein
Biological processCell cycle, Cell division
LigandChitin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chondroitin proteoglycan 1
Alternative name(s):
Cell junction protein 1
Cytokinesis protein cej-1
Gene namesi
Name:cpg-1
ORF Names:CBG03957
OrganismiCaenorhabditis briggsae
Taxonomic identifieri6238 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000008549 Componentsi: Chromosome I, Unassembled WGS sequence

Organism-specific databases

WormBaseiCBG03957a ; CBP41672 ; WBGene00026714 ; Cbr-cpg-1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000032021919 – 686Chondroitin proteoglycan 1Add BLAST668

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi46N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi96 ↔ 109PROSITE-ProRule annotation
Glycosylationi143N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi261 ↔ 274PROSITE-ProRule annotation
Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi635N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi664N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Structurei

3D structure databases

ProteinModelPortaliA8WVU7
SMRiA8WVU7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 120Chitin-binding type-2 1PROSITE-ProRule annotationAdd BLAST58
Domaini228 – 285Chitin-binding type-2 2PROSITE-ProRule annotationAdd BLAST58

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi316 – 592Thr-richSequence analysisAdd BLAST277

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IN9E Eukaryota
ENOG4111RTJ LUCA
HOGENOMiHOG000111921
InParanoidiA8WVU7
OMAiTTVGYEP
OrthoDBiEOG091G0JFK

Family and domain databases

InterProiView protein in InterPro
IPR002557 Chitin-bd_dom
IPR036508 Chitin-bd_dom_sf
PfamiView protein in Pfam
PF01607 CBM_14, 2 hits
SMARTiView protein in SMART
SM00494 ChtBD2, 2 hits
SUPFAMiSSF57625 SSF57625, 2 hits
PROSITEiView protein in PROSITE
PS50940 CHIT_BIND_II, 2 hits

Sequencei

Sequence statusi: Complete.

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

A8WVU7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPKSVLIVA FLVASSSAQY GVTGMYENLP LESTTVEASG EGSGYNESND
60 70 80 90 100
DGFVTGADAV AIDTDCSTKE DGLYAIGGCS PQFLTCSGGI ARIMDCPANL
110 120 130 140 150
IYDQRIIACE YSYNVPECSG VPQDVSSTQA YYPATEETTP AENVTVPAET
160 170 180 190 200
TVDPYAPVEV ATTAAPSEDV PVETTASPYA PVEVETTTAP AEDVTVPEET
210 220 230 240 250
TVAPYAPVEV YTTAAPANDE PVTRTLLDKT CNGKADGFYS FGQCSDHYIA
260 270 280 290 300
CSNGYTIPMQ CPARLSFDEA RVICDYTMNV PECQNGSGNY EGSAEETTTE
310 320 330 340 350
ASGELPYSNG YGYEETTTAA ADVPSTEGYA PETTAEAWVA PYRLESTTAA
360 370 380 390 400
DVPTTTVGYA PEVIEETTTS EYVEETTTAA DVSTTTTVEY VPEVTETTTA
410 420 430 440 450
PYVEETTTAE YVEETTTAAD VPTTTTVAYA PEVTETTTVP YIEETTTVEE
460 470 480 490 500
ATTAADVPTT TGYVPEVIET TTTPYVEETT TAEYVEETST AADVPTTTTV
510 520 530 540 550
AYAPEVTETT TVPYIEETTT VEEATTAADV PTTTGYVPEV IETTTTPYVE
560 570 580 590 600
ETTTVEETTT TTVAYAPEVV ETTTTPYVEE STTTPYVEET TTALMFHPPQ
610 620 630 640 650
SKATKLPQIH HPASKEHLLS SHAHKTIETV SMDMNLSSSA SRDSSSLQSK
660 670 680
DDAQLLTKLR SATNRTSTKE ATTRTQNMHA HYHRNH
Length:686
Mass (Da):73,321
Last modified:January 15, 2008 - v1
Checksum:i6C43466951D120A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE600906 Genomic DNA Translation: CAP24760.1
RefSeqiXP_002639373.1, XM_002639327.1

Genome annotation databases

GeneIDi8581366
KEGGicbr:CBG03957

Similar proteinsi

Entry informationi

Entry nameiCPG1_CAEBR
AccessioniPrimary (citable) accession number: A8WVU7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: January 15, 2008
Last modified: March 28, 2018
This is version 52 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health