GenomeNet

Database: UniProt
Entry: Q28858
LinkDB: Q28858
Original site: Q28858 
ID   CSPG2_MACNE             Reviewed;         862 AA.
AC   Q28858; Q28859; Q28860;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   20-JUN-2018, entry version 104.
DE   RecName: Full=Versican core protein;
DE   AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
DE            Short=Chondroitin sulfate proteoglycan 2;
DE   AltName: Full=Large fibroblast proteoglycan;
DE   Flags: Fragments;
GN   Name=VCAN; Synonyms=CSPG2;
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aortic smooth muscle;
RX   PubMed=7921538; DOI=10.1016/0945-053X(94)90185-6;
RA   Yao L.Y., Moody C., Schoenherr E., Wight T.N., Sandell L.J.;
RT   "Identification of the proteoglycan versican in aorta and smooth
RT   muscle cells by DNA sequence analysis, in situ hybridization and
RT   immunohistochemistry.";
RL   Matrix Biol. 14:213-225(1994).
CC   -!- FUNCTION: May play a role in intercellular signaling and in
CC       connecting cells with the extracellular matrix. May take part in
CC       the regulation of cell motility, growth and differentiation. Binds
CC       hyaluronan.
CC   -!- SUBUNIT: Interacts with FBLN1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Disappears after the cartilage development.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P13611}.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
DR   EMBL; S72412; AAA65593.2; -; mRNA.
DR   EMBL; S72413; AAA65594.2; -; mRNA.
DR   EMBL; S72414; AAA65595.2; -; mRNA.
DR   PIR; S43922; S43922.
DR   ProteinModelPortal; Q28858; -.
DR   SMR; Q28858; -.
DR   Proteomes; UP000233120; Whole Genome Shotgun Assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 3.10.100.10; -; 3.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
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; IPR000538; Link_dom.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00445; LINK; 1.
DR   SUPFAM; SSF56436; SSF56436; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Complete proteome; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Lectin; Phosphoprotein;
KW   Proteoglycan; Reference proteome; Repeat; Secreted.
FT   CHAIN        <1   >862       Versican core protein.
FT                                /FTId=PRO_0000046693.
FT   DOMAIN       <1     38       Link 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN       44    140       Link 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      718    754       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      756    792       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      805   >862       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   REGION      141   >233       GAG-alpha (glucosaminoglycan attachment
FT                                domain).
FT   REGION     <234   >525       Glucosaminoglycan attachment domain,
FT                                similar to chondroitin sulfate attachment
FT                                site in collagen type IX. {ECO:0000250}.
FT   MOD_RES     269    269       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13611}.
FT   CARBOHYD    123    123       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    332    332       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    425    425       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    477    477       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    513    513       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    563    563       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    696    696       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     63    138       {ECO:0000250}.
FT   DISULFID     87    108       {ECO:0000250}.
FT   DISULFID    722    733       {ECO:0000250}.
FT   DISULFID    727    742       {ECO:0000250}.
FT   DISULFID    744    753       {ECO:0000250}.
FT   DISULFID    760    771       {ECO:0000250}.
FT   DISULFID    765    780       {ECO:0000250}.
FT   DISULFID    782    791       {ECO:0000250}.
FT   NON_CONS    233    234       {ECO:0000305}.
FT   NON_CONS    525    526       {ECO:0000305}.
FT   NON_TER       1      1
FT   NON_TER     862    862
SQ   SEQUENCE   862 AA;  95583 MW;  A5D5F6153A74BB39 CRC64;
     YPIRAPRVGC YGDMMGKAGV RTYGFRSPQE TYDVYCYVDH LDGDVFHLTA PSKFTFEEAA
     KECENQDARL ATVGELQAAW RNGFDQCDYG WLSDASVRHP VTVARAQCGG GLLGVRTLYR
     FENQTGFPPP DSRFDAYCFK RRMSDLSVIG HPIDSESKED EPCSEETDPV HDLMAEILPE
     FPDIIEIDLY HSEENEEEEE ECANATDVTT TPSVQYINGK HLVTTVPKDP EAASGTISTN
     FPQTMEPAKL WSRQEVNPER QEIESETTSE EQIQEEKSFE SPQNSPATEQ TIFDSQTFTE
     TELKTTGYSV LTTKKTYSDD KEMEEEGTSL ANMSTPVPDA NGVESFTTLP EATEKSHFFL
     ATALVTESIP AEHVVTDSPI KEEESTKHFP KGMRPTIQEL DTELLFSGLG SGEEVLPTLP
     TKSVNFTEVE QIRNTFYPHT SQVESTSSDK LEDFNRMENV AKEVGPLGSQ TDIFEGNESV
     TSTTLIEILS DPGAEGPTVA PLPFFANIGH PQNQTLRWAE EIQTSKLEPS EEDGKPELLE
     ETEASPTEFI AVEGTEILQD FQNKTDGQVS GEAIKMFPTI KTPEAGTVIT TANEIKLEGA
     TQWPHSTSAS ATYGIEAGVM PWLSPQTSER PTLSSSPEIN PETQAALIRG QDSTVAASEQ
     QVTARILDTN DQATVSPVEF NTEVATPPFS LLETSNETDF LIGINEESVE GTAIYLPGPD
     RCKMNPCLNG GTCYPTETSY VCTCVPGYSG DQCELDFDEC HSNPCRNGAT CADGFNTFRC
     LCLPSYVGAL CEQDIETCDY GWHKFQGQCY KYFAHRRTWD AAERECRLQG AHLTSILSHE
     EQMFVNRVGH DYQWIGLNDK MF
//
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