ID Q4LE67_HUMAN Unreviewed; 1335 AA.
AC Q4LE67;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 24-JAN-2024, entry version 146.
DE SubName: Full=CSPG3 variant protein {ECO:0000313|EMBL:BAE06086.1};
DE Flags: Fragment;
GN Name=CSPG3 variant protein {ECO:0000313|EMBL:BAE06086.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAE06086.1};
RN [1] {ECO:0000313|EMBL:BAE06086.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:BAE06086.1};
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB210004; BAE06086.1; -; mRNA.
DR RefSeq; NP_004377.2; NM_004386.2.
DR PeptideAtlas; Q4LE67; -.
DR DNASU; 1463; -.
DR GeneID; 1463; -.
DR KEGG; hsa:1463; -.
DR CTD; 1463; -.
DR PharmGKB; PA162396986; -.
DR OrthoDB; 5402504at2759; -.
DR PhylomeDB; Q4LE67; -.
DR BioGRID-ORCS; 1463; 17 hits in 1145 CRISPR screens.
DR ChiTaRS; NCAN; human.
DR GenomeRNAi; 1463; -.
DR Genevisible; Q4LE67; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd05902; Ig_Neurocan; 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; 2.
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; 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; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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:SF24; NEUROCAN 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; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00409; IG; 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; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..167
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 174..269
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 273..371
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1022..1058
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1060..1096
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1109..1223
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1227..1287
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 376..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1320
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 220..241
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 318..339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1048..1057
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1086..1095
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1229..1272
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1258..1285
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAE06086.1"
SQ SEQUENCE 1335 AA; 144643 MW; 4560E9CE87A699A7 CRC64;
RPPRDASELG ARSRMGAPFV WALGLLMLQM LLFVAGEQGT QDITDASERG LHMQKLGSGS
VQAALAELVA LPCLFTLQPR PSAARDAPRI KWTKVRTASG QRQDLPILVA KDNVVRVAKS
WQGRVSLPSY PRRRANATLL LGPLRASDSG LYRCQVVRGI EDEQDLVPLE VTGVVFHYRS
ARDRYALTFA EAQEACRLSS AIIAAPRHLQ AAFEDGFDNC DAGWLSDRTV RYPITQSRPG
CYGDRSSLPG VRSYGRRNPQ ELYDVYCFAR ELGGEVFYVG PARRLTLAGA RAQCRRQGAA
LASVGQLHLA WHEGLDQCDP GWLADGSVRY PIQTPRRRCG GPAPGVRTVY RFANRTGFPS
PAERFDAYCF RAHHPTSQHG DLETPSSGDE GEILSAEGPP VRELEPTLEE EEVVTPDFQE
PLVSSGEEET LILEEKQESQ QTLSPTPGDP MLASWPTGEV WLSTVAPSPS DMGAGTAASS
HTEVAPTDPM PRRRGRFKGL NGRYFQQQEP EPGLQGGMEA SAQPPTSEAA VNQMEPPLAM
AVTEMLGSGQ SRSPWADLTN EVDMPGAGSA GGKSSPEPWL WPPTMVPPSI SGHSRAPVLE
LEKAEGPSAR PATPDLFWSP LEATVSAPSP APWEAFPVAT SPDLPMMAML RGPKEWMLPH
PTPISTEANR VEAHGEATAT APPSPAAETK VYSLPLSLTP TGQGGEAMPT TPESPRADFR
ETGETSPAQV NKAEHSSSSP WPSVNRNVAV GFVPTETATE PTGLRGIPGS ESGVFDTAES
PTSGLQATVD EVQDPWPSVY SKGLDASSPS APLGSPGVFL VPKVTPNLEP WVATDEGPTV
NPMDSTVTPA PSDASGIWEP GSQVFEEAES TTLSPQVALD TSIVTPLTTL EQGDKVGVPA
MSTLGSSSSQ PHPEPEDQVE TQGTSGASVP PHQSSPLGKP AVPPGTPTAA SVGESASVSS
GEPTVPWDPS STLLPVTLGI EDFELEVLAG SPGVESFWEE VASGEEPALP GTPMNAGAEE
VHSDPCENNP CLHGGTCNAN GTMYGCSCDQ GFAGENCEID IDDCLCSPCE NGGTCIDEVN
GFVCLCLPSY GGSFCEKDTE GCDRGWHKFQ GHCYRYFAHR RAWEDAEKDC RRRSGHLTSV
HSPEEHSFIN SFGHENTWIG LNDRIVERDF QWTDNTGLQF ENWRENQPDN FFAGGEDCVV
MVAHESGRWN DVPCNYNLPY VCKKGTVLCG PPPAVENASL IGARKAKYNV HATVRYQCNE
GFAQHHVATI RCRSNGKWDR PQIVCTKPRR SHRMRRHHHH HQHHHQHHHH KSRKERRKHK
KHPTEDWEKD EGNFC
//
