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PGCB_FELCA
ID   PGCB_FELCA              Reviewed;         417 AA.
AC   P41725;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   23-FEB-2022, entry version 114.
DE   RecName: Full=Brevican core protein;
DE   AltName: Full=Brain-enriched hyaluronan-binding protein;
DE            Short=BEHAB;
DE   Flags: Precursor; Fragment;
GN   Name=BCAN;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7512973; DOI=10.1083/jcb.125.2.495;
RA   Jaworski D.M., Kelly G.M., Hockfield S.;
RT   "BEHAB, a new member of the proteoglycan tandem repeat family of
RT   hyaluronan-binding proteins that is restricted to the brain.";
RL   J. Cell Biol. 125:495-509(1994).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RX   PubMed=7488217; DOI=10.1006/bbrc.1995.2713;
RA   Yamada H., Watanabe K., Shimonaka M., Yamasaki M., Yamaguchi Y.;
RT   "cDNA cloning and the identification of an aggrecanase-like cleavage site
RT   in rat brevican.";
RL   Biochem. Biophys. Res. Commun. 216:957-963(1995).
CC   -!- FUNCTION: May play a role in the terminally differentiating and the
CC       adult nervous system during postnatal development. Could stabilize
CC       interactions between hyaluronan (HA) and brain proteoglycans.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Central nervous system.
CC   -!- PTM: Contains mostly chondroitin sulfate.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA82216.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z28367; CAA82216.1; ALT_FRAME; mRNA.
DR   PIR; I46268; I46268.
DR   STRING; 9685.ENSFCAP00000006092; -.
DR   PRIDE; P41725; -.
DR   InParanoid; P41725; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.100.10; -; 2.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000538; Link_dom.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF56436; SSF56436; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
DR   PROSITE; PS01241; LINK_1; 2.
DR   PROSITE; PS50963; LINK_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW   Immunoglobulin domain; Proteoglycan; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..>417
FT                   /note="Brevican core protein"
FT                   /id="PRO_0000017510"
FT   DOMAIN          23..155
FT                   /note="Ig-like V-type"
FT   DOMAIN          157..252
FT                   /note="Link 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   DOMAIN          257..354
FT                   /note="Link 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        179..250
FT                   /evidence="ECO:0000250"
FT   DISULFID        203..224
FT                   /evidence="ECO:0000250"
FT   DISULFID        277..352
FT                   /evidence="ECO:0000250"
FT   DISULFID        301..322
FT                   /evidence="ECO:0000250"
FT   NON_TER         417
SQ   SEQUENCE   417 AA;  44989 MW;  BDFAAADFC8A1E6A9 CRC64;
     MAPLFLPLLI ALALAPGPTA SADVLEGDSS EDRAFRVRIS GNAPLQGVLG GALTISCHVH
     YLRPPPGRRA VLGSPRVKWT FLSGGREAEV LVARGLRVKV SEAYRFRVAL PAYPASLTDV
     SLALSELRPN DSGIYRCEVQ HGIDDSSDAV EVKVKGVVFL YREGSARYAF SFARAQEACA
     RIGARIATPE QLYAAYLGGY EQCDAGWLSD QTVRYPIQTP REACYGDMDG FPGVRNYGLV
     DPDDLYDIYC YAEDLNGELF LGAPPDNVTL EEATAYCRER GAEIATTGQL YAAWDGGLDR
     CSPGWLADGS VRYPIVTPSQ RCGGGLPGVK TLFLFPNQTG FPNKYSRFNV YCFRDSGQPS
     TTPEASXPAS DGLEAIVTVT ETLEELHVPR EAVESESRGA IYSVPIVEDG GGARSPP
 
 
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