CSPG2_MACNE
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 25-MAY-2022, entry version 115.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC 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 muscle
RT 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 connecting
CC cells with the extracellular matrix. May take part in the regulation of
CC cell motility, growth and differentiation. Binds hyaluronan.
CC -!- SUBUNIT: Interacts with FBLN1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P13611}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:P13611}. Secreted,
CC extracellular space, extracellular matrix, interphotoreceptor matrix
CC {ECO:0000250|UniProtKB:P13611}.
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}.
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DR EMBL; S72412; AAA65593.2; -; mRNA.
DR EMBL; S72413; AAA65594.2; -; mRNA.
DR EMBL; S72414; AAA65595.2; -; mRNA.
DR PIR; S43922; S43922.
DR AlphaFoldDB; Q28858; -.
DR SMR; Q28858; -.
DR STRING; 9545.ENSMNEP00000026950; -.
DR Proteomes; UP000233120; Whole Genome Shotgun Assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
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; -; 2.
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; 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; Cell projection; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Lectin; Phosphoprotein; Proteoglycan;
KW Reference proteome; Repeat; Secreted.
FT CHAIN <1..>862
FT /note="Versican core protein"
FT /id="PRO_0000046693"
FT DOMAIN <1..38
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 44..140
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 718..754
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 756..792
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 805..>862
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 141..>233
FT /note="GAG-alpha (glucosaminoglycan attachment domain)"
FT REGION <234..>525
FT /note="Glucosaminoglycan attachment domain, similar to
FT chondroitin sulfate attachment site in collagen type IX"
FT /evidence="ECO:0000250"
FT REGION 251..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13611"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..138
FT /evidence="ECO:0000250"
FT DISULFID 87..108
FT /evidence="ECO:0000250"
FT DISULFID 722..733
FT /evidence="ECO:0000250"
FT DISULFID 727..742
FT /evidence="ECO:0000250"
FT DISULFID 744..753
FT /evidence="ECO:0000250"
FT DISULFID 760..771
FT /evidence="ECO:0000250"
FT DISULFID 765..780
FT /evidence="ECO:0000250"
FT DISULFID 782..791
FT /evidence="ECO:0000250"
FT NON_CONS 233..234
FT /evidence="ECO:0000305"
FT NON_CONS 525..526
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 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
