PGCB_HUMAN
ID PGCB_HUMAN Reviewed; 911 AA.
AC Q96GW7; D3DVC2; Q5SZ10; Q5T3I5; Q8TBB9; Q9HBK1; Q9HBK4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Brevican core protein;
DE AltName: Full=Brain-enriched hyaluronan-binding protein;
DE Short=BEHAB;
DE AltName: Full=Chondroitin sulfate proteoglycan 7;
DE Flags: Precursor;
GN Name=BCAN; Synonyms=BEHAB, CSPG7; ORFNames=UNQ2525/PRO6018;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain cortex;
RX PubMed=11054543; DOI=10.1016/s0378-1119(00)00362-0;
RA Gary S.C., Zerillo C.A., Chiang V.L., Gaw J.U., Gray G., Hockfield S.;
RT "cDNA cloning, chromosomal localization, and expression analysis of human
RT BEHAB/brevican, a brain specific proteoglycan regulated during cortical
RT development and in glioma.";
RL Gene 256:139-147(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-504.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-906, AND STRUCTURE
RP OF CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA Lako M.;
RT "Extracellular matrix component expression in human pluripotent stem cell-
RT derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT an important role for IMPG1 and CD44 in the development of photoreceptors
RT and interphotoreceptor matrix.";
RL Acta Biomater. 74:207-221(2018).
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 -!- SUBUNIT: Interacts with TNR. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96GW7; Q06481-5: APLP2; NbExp=3; IntAct=EBI-2690445, EBI-25646567;
CC Q96GW7; P05067: APP; NbExp=3; IntAct=EBI-2690445, EBI-77613;
CC Q96GW7; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-2690445, EBI-9087876;
CC Q96GW7; P07948: LYN; NbExp=3; IntAct=EBI-2690445, EBI-79452;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space,
CC extracellular matrix.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96GW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96GW7-2; Sequence=VSP_011184, VSP_011185;
CC -!- TISSUE SPECIFICITY: Expressed in the retina, specifically in the inner
CC nuclear layer, inner plexiform layer and ganglion cell layer (at
CC protein level). {ECO:0000269|PubMed:29777959}.
CC -!- DEVELOPMENTAL STAGE: Expressed between 6 and 19 weeks post-conception
CC (WPC) in the outer neuroblastic zone, inner neuroblastic zone, and
CC inner plexiform layer of the retina (at protein level)
CC (PubMed:29777959). Expressed at the surface ectoderm at 6 WPC and the
CC neural retinal at 6 to 8 WPC (at protein level) (PubMed:29777959).
CC Expressed in the interphotoreceptor matrix and abundantly in developing
CC photoreceptors between 12 and 19 WPC (at protein level)
CC (PubMed:29777959). Isoform 1: Highly expressed from birth through 8
CC years of age and is down-regulated by 20 years of age to low levels
CC that are maintained in the normal adult cortex (PubMed:11054543).
CC Isoform 2: Expressed at uniformly low levels throughout development
CC (PubMed:11054543). {ECO:0000269|PubMed:11054543,
CC ECO:0000269|PubMed:29777959}.
CC -!- PTM: Contains mostly chondroitin sulfate (By similarity). O-
CC glycosylated with a core 1 or possibly core 8 glycan. {ECO:0000250,
CC ECO:0000269|PubMed:19838169}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Brevican;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_212";
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; AF228710; AAG23134.1; -; mRNA.
DR EMBL; AF229053; AAG23135.1; -; mRNA.
DR EMBL; AY358372; AAQ88738.1; -; mRNA.
DR EMBL; AL365181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52927.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52928.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52929.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52930.1; -; Genomic_DNA.
DR EMBL; BC009117; AAH09117.1; -; mRNA.
DR EMBL; BC022938; AAH22938.1; -; mRNA.
DR EMBL; BC027971; AAH27971.1; -; mRNA.
DR CCDS; CCDS1149.1; -. [Q96GW7-1]
DR CCDS; CCDS1150.1; -. [Q96GW7-2]
DR RefSeq; NP_068767.3; NM_021948.4. [Q96GW7-1]
DR RefSeq; NP_940819.1; NM_198427.1. [Q96GW7-2]
DR RefSeq; XP_011508168.1; XM_011509866.1. [Q96GW7-1]
DR AlphaFoldDB; Q96GW7; -.
DR SMR; Q96GW7; -.
DR BioGRID; 121964; 43.
DR IntAct; Q96GW7; 10.
DR STRING; 9606.ENSP00000331210; -.
DR GlyGen; Q96GW7; 7 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q96GW7; -.
DR PhosphoSitePlus; Q96GW7; -.
DR BioMuta; BCAN; -.
DR DMDM; 68067899; -.
DR jPOST; Q96GW7; -.
DR MassIVE; Q96GW7; -.
DR PaxDb; Q96GW7; -.
DR PeptideAtlas; Q96GW7; -.
DR PRIDE; Q96GW7; -.
DR ProteomicsDB; 76671; -. [Q96GW7-1]
DR ProteomicsDB; 76672; -. [Q96GW7-2]
DR TopDownProteomics; Q96GW7-2; -. [Q96GW7-2]
DR ABCD; Q96GW7; 4 sequenced antibodies.
DR Antibodypedia; 2188; 198 antibodies from 29 providers.
DR DNASU; 63827; -.
DR Ensembl; ENST00000329117.10; ENSP00000331210.4; ENSG00000132692.19. [Q96GW7-1]
DR Ensembl; ENST00000361588.5; ENSP00000354925.5; ENSG00000132692.19. [Q96GW7-2]
DR GeneID; 63827; -.
DR KEGG; hsa:63827; -.
DR MANE-Select; ENST00000329117.10; ENSP00000331210.4; NM_021948.5; NP_068767.3.
DR UCSC; uc001fpo.4; human. [Q96GW7-1]
DR CTD; 63827; -.
DR DisGeNET; 63827; -.
DR GeneCards; BCAN; -.
DR HGNC; HGNC:23059; BCAN.
DR HPA; ENSG00000132692; Tissue enriched (brain).
DR MIM; 600347; gene.
DR neXtProt; NX_Q96GW7; -.
DR OpenTargets; ENSG00000132692; -.
DR PharmGKB; PA134868393; -.
DR VEuPathDB; HostDB:ENSG00000132692; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000157343; -.
DR HOGENOM; CLU_000303_0_0_1; -.
DR InParanoid; Q96GW7; -.
DR OMA; APQISCV; -.
DR OrthoDB; 174823at2759; -.
DR PhylomeDB; Q96GW7; -.
DR TreeFam; TF332134; -.
DR PathwayCommons; Q96GW7; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-HSA-2024101; CS/DS degradation.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
DR Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type.
DR Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR SignaLink; Q96GW7; -.
DR BioGRID-ORCS; 63827; 61 hits in 1079 CRISPR screens.
DR ChiTaRS; BCAN; human.
DR GeneWiki; Brevican; -.
DR GenomeRNAi; 63827; -.
DR Pharos; Q96GW7; Tbio.
DR PRO; PR:Q96GW7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96GW7; protein.
DR Bgee; ENSG00000132692; Expressed in ventricular zone and 158 other tissues.
DR ExpressionAtlas; Q96GW7; baseline and differential.
DR Genevisible; Q96GW7; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
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: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:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 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 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; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 3.
DR SUPFAM; SSF57535; SSF57535; 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; 2.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; GPI-anchor; Hyaluronic acid;
KW Immunoglobulin domain; Lectin; Lipoprotein; Membrane; Phosphoprotein;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..911
FT /note="Brevican core protein"
FT /id="PRO_0000017511"
FT DOMAIN 36..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 DOMAIN 646..682
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 695..809
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 813..873
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 391..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..530
FT /note="O-glycosylated at two sites"
FT REGION 540..545
FT /note="O-glycosylated at two sites"
FT REGION 569..575
FT /note="O-glycosylated at one site"
FT COMPBIAS 453..479
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55068"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 905
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000305|PubMed:19838169"
FT CARBOHYD 906
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000305|PubMed:19838169"
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 DISULFID 650..661
FT /evidence="ECO:0000250"
FT DISULFID 655..670
FT /evidence="ECO:0000250"
FT DISULFID 672..681
FT /evidence="ECO:0000250"
FT DISULFID 688..699
FT /evidence="ECO:0000250"
FT DISULFID 716..808
FT /evidence="ECO:0000250"
FT DISULFID 784..800
FT /evidence="ECO:0000250"
FT DISULFID 815..858
FT /evidence="ECO:0000250"
FT DISULFID 844..871
FT /evidence="ECO:0000250"
FT VAR_SEQ 649..671
FT /note="DCVPSPCHNGGTCLEEEEGVRCL -> NSAQGSTALSILLLFFPLQLWVT
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11054543"
FT /id="VSP_011184"
FT VAR_SEQ 672..911
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11054543"
FT /id="VSP_011185"
FT VARIANT 356
FT /note="S -> L (in dbSNP:rs12065791)"
FT /id="VAR_050123"
FT VARIANT 504
FT /note="E -> K (in dbSNP:rs1056695)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_019551"
FT CONFLICT 175
FT /note="A -> T (in Ref. 5; AAH22938)"
FT /evidence="ECO:0000305"
FT LIPID Q96GW7-2:646
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 911 AA; 99118 MW; 5268E796FA3938D2 CRC64;
MAQLFLPLLA ALVLAQAPAA LADVLEGDSS EDRAFRVRIA GDAPLQGVLG GALTIPCHVH
YLRPPPSRRA VLGSPRVKWT FLSRGREAEV LVARGVRVKV NEAYRFRVAL PAYPASLTDV
SLALSELRPN DSGIYRCEVQ HGIDDSSDAV EVKVKGVVFL YREGSARYAF SFSGAQEACA
RIGAHIATPE QLYAAYLGGY EQCDAGWLSD QTVRYPIQTP REACYGDMDG FPGVRNYGVV
DPDDLYDVYC YAEDLNGELF LGDPPEKLTL EEARAYCQER GAEIATTGQL YAAWDGGLDH
CSPGWLADGS VRYPIVTPSQ RCGGGLPGVK TLFLFPNQTG FPNKHSRFNV YCFRDSAQPS
AIPEASNPAS NPASDGLEAI VTVTETLEEL QLPQEATESE SRGAIYSIPI MEDGGGGSST
PEDPAEAPRT LLEFETQSMV PPTGFSEEEG KALEEEEKYE DEEEKEEEEE EEEVEDEALW
AWPSELSSPG PEASLPTEPA AQEESLSQAP ARAVLQPGAS PLPDGESEAS RPPRVHGPPT
ETLPTPRERN LASPSPSTLV EAREVGEATG GPELSGVPRG ESEETGSSEG APSLLPATRA
PEGTRELEAP SEDNSGRTAP AGTSVQAQPV LPTDSASRGG VAVVPASGDC VPSPCHNGGT
CLEEEEGVRC LCLPGYGGDL CDVGLRFCNP GWDAFQGACY KHFSTRRSWE EAETQCRMYG
AHLASISTPE EQDFINNRYR EYQWIGLNDR TIEGDFLWSD GVPLLYENWN PGQPDSYFLS
GENCVVMVWH DQGQWSDVPC NYHLSYTCKM GLVSCGPPPE LPLAQVFGRP RLRYEVDTVL
RYRCREGLAQ RNLPLIRCQE NGRWEAPQIS CVPRRPARAL HPEEDPEGRQ GRLLGRWKAL
LIPPSSPMPG P
