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Database: UniProt
Entry: A4IF65_BOVIN
LinkDB: A4IF65_BOVIN
Original site: A4IF65_BOVIN 
ID   A4IF65_BOVIN            Unreviewed;       672 AA.
AC   A4IF65;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Brevican core protein {ECO:0000256|ARBA:ARBA00044100};
GN   Name=BCAN {ECO:0000313|EMBL:AAI34426.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI34426.1};
RN   [1] {ECO:0000313|EMBL:AAI34426.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hereford {ECO:0000313|EMBL:AAI34426.1};
RC   TISSUE=Hypothalamus {ECO:0000313|EMBL:AAI34426.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000256|ARBA:ARBA00006838}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00323}.
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DR   EMBL; BC134425; AAI34426.1; -; mRNA.
DR   RefSeq; NP_001231054.1; NM_001244125.1.
DR   AlphaFoldDB; A4IF65; -.
DR   GeneID; 281019; -.
DR   KEGG; bta:281019; -.
DR   CTD; 63827; -.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1.
DR   CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR   PANTHER; PTHR22804:SF41; BREVICAN CORE PROTEIN; 1.
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; SSF56436; C-type lectin-like; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00323};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..672
FT                   /note="Brevican core protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002670483"
FT   DOMAIN          50..155
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          157..252
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          257..354
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   REGION          438..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..479
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..541
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        203..224
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        301..322
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ   SEQUENCE   672 AA;  72137 MW;  7D4C33C3EA8C15BB CRC64;
     MAPLFLPLLA TLVLAWIPVA LADALEGDSS EDRAFRVRIA GDAPLQGVLG GALTIPCHVH
     YLRPSPSRRA AQGSPRVKWT FLSGGREAEV LVARGLRVKV SEAYRFRVAL PAYPASLTDV
     SLVLSELRPN DSGIYRCEVQ HGIDDSSDAV EVKVKGVVFL YREGSARYAF SFAGAQEACA
     RIGARIATPE QLYAAYLGGY EQCDAGWLSD QTVRYPIQTP REACYGDMDG FPGVRNYGVV
     DPDDLYDVYC YAEELNGELF LGAPPDKLTL EEARTYCQER GAKIATTGQL YAAWDGGLDR
     CSPGWLADGS VRYPIVTPSQ RCGGGLPGVK TLFLFPNQTG FPNKHSRFNV YCFRDSAQPS
     AIPEAANPAS HLASDALEAI VTVTETLEEL KLPQEAVESE SRGAIYSIPI IEDGGGGSST
     PEDPAEAPRT LLEFKTQSIV PPLGSSEEEG KVLEQEEKYR GEEEKEEEEE EEEVEDEALW
     AWPSELSSLD PEAPLPTEPV PEESLTQASP PVRAALQPGV SPPAYDEPEA PRPPRVLGPP
     TKTLPTPREG NLASPPPSTL VGAREIEEET GGPELSGAPR GESEETGSSE DAPSLLPATR
     APGDTRDLET PSEENSRRTV PAGTSVRAQP VLPTDSASRG GVAVAPSSGN FAQGSASLLL
     LLLFLPLQLW IT
//
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