ID U3EKU7_CALJA Unreviewed; 908 AA.
AC U3EKU7; A0A2R8PN17; F7ISR3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Brevican core protein {ECO:0000256|ARBA:ARBA00044100};
GN Name=BCAN {ECO:0000313|EMBL:JAB22540.1,
GN ECO:0000313|Ensembl:ENSCJAP00000011200.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB22540.1};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000011200.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB22540.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Hippocampus {ECO:0000313|EMBL:JAB22540.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000011200.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:PRU00076}.
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DR EMBL; GAMS01000598; JAB22538.1; -; mRNA.
DR EMBL; GAMS01000596; JAB22540.1; -; mRNA.
DR STRING; 9483.ENSCJAP00000011200; -.
DR Ensembl; ENSCJAT00000011820.5; ENSCJAP00000011200.3; ENSCJAG00000006078.5.
DR Ensembl; ENSCJAT00000083233.3; ENSCJAP00000067316.2; ENSCJAG00000006078.5.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000157343; -.
DR HOGENOM; CLU_000303_0_1_1; -.
DR OMA; APQISCV; -.
DR TreeFam; TF332134; -.
DR Proteomes; UP000008225; Chromosome 18.
DR Bgee; ENSCJAG00000006078; Expressed in frontal cortex and 3 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR GO; GO:0072534; C:perineuronal net; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1.
DR CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
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 InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR PANTHER; PTHR22804:SF41; BREVICAN CORE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 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.
DR PROSITE; PS50923; SUSHI; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW Immunity {ECO:0000256|ARBA:ARBA00022451};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW MHC I {ECO:0000256|ARBA:ARBA00022451};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..908
FT /note="Brevican core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015101490"
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 DOMAIN 643..679
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 692..806
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 810..870
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 435..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..479
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..537
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"
FT DISULFID 669..678
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 812..855
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 841..868
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 908 AA; 98335 MW; EE6BD08265774460 CRC64;
MAQLLLLLLA ALVLAQVPAA LADVLEGDSS EDRAFRVRIS GDAPLQGVLG GALTIPCHVH
YLRPPPSRRA VLGSPRVKWT FLSGGREAEV LVARGVRVKV NEAYRFRVAL PAYPASLTDV
SLALSELRPN DSGIYRCEVQ HGIDDSSDAV EVKVKGVVFL YREGSARYAF SFVGAQEACA
RIGAHIATPE QLYAAYLGGY EQCDAGWLSD QTVRYPIQTP REACYGDMDG FPGVRNYGVV
DPDDLYDVYC YAADLNGELF LGDPPEKLTL EEARAYCQQR GAEIATTGQL YAAWDGGLDH
CSPGWLADGS VRYPIVTPSQ RCGGGLPGVK TLFLFPNQTG FPNKHSRFNV YCFRDSAQPS
AITEAANPAS DPASDGLEAI VTVTETLEEL QLPQEAMESE SRGAIYSIPI MEDGGGGSST
PEDPAEAPRT ILEFETQSMV PPTGFSEEEG KALEEEEKYG DEEEKEEEEE EEEVDDEALW
AWPSELSSPG PETSLPTEPA DQEESFSQAP AKAVLHPGAS PLPDGGPRPP RVHGPPTETL
PTPREGNLAS PSPSTLVGAR EVGEETGGPD LSGVPRGESE EMGSSEDAPS LLPATRAPEG
ARELEAPSED NSGRTAPAGT SVQAQPVLPT DSASRGGVAV VLATGDCVPS PCHNGGTCLE
VEGKVHCLCL PGYGGDLCDV GLHFCSPGWE AFQGSCYKHF STRRSWEDAE TQCRMYGAHL
ASISTPEEQD FINNRYREYQ WIGLNDRTIE GDFLWSDGVP LLYENWNPGQ PDSYFLSGEN
CVVMVWHDQG QWSDVPCNYH LSYTCKMGLV SCGPPPELPL AQVFGRPRLR YEVDTVLRYR
CREGLAQRNL PLIRCQKNGR WRTPQISCVP QRPAGALHPE KAPEGPQGRL LGRWKALLTP
PSSPTPGP
//
