CBPD_DROME
ID CBPD_DROME Reviewed; 1406 AA.
AC P42787; A2RVE4; B7Z112; C7LAH0; D0Z763; O46058; Q24094; Q24095; Q9W5F3;
AC Q9W5F4; Q9W5F5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Carboxypeptidase D;
DE EC=3.4.17.22;
DE AltName: Full=Metallocarboxypeptidase D;
DE AltName: Full=Protein silver;
DE Flags: Precursor;
GN Name=svr; Synonyms=CPD, CpepE; ORFNames=CG4122;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 5; 6 AND 7), AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=12393882; DOI=10.1074/jbc.m209652200;
RA Sidyelyeva G., Fricker L.D.;
RT "Characterization of Drosophila carboxypeptidase D.";
RL J. Biol. Chem. 277:49613-49620(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Booth B., Frise E., Kapadia B., Park S.,
RA Wan K.H., Yu C., Celniker S.E.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1152 (ISOFORMS 1/5), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 93-152 (ISOFORMS 3/4/6), AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=7568156; DOI=10.1073/pnas.92.21.9470;
RA Settle S.H. Jr., Green M.M., Burtis K.C.;
RT "The silver gene of Drosophila melanogaster encodes multiple
RT carboxypeptidases similar to mammalian prohormone-processing enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9470-9474(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 425-696, FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Canton-S;
RX PubMed=8000074; DOI=10.1002/arch.940270303;
RA Bernasconi P.;
RT "Molecular cloning of a Drosophila melanogaster gene coding for an
RT homologue of human carboxypeptidase E.";
RL Arch. Insect Biochem. Physiol. 27:169-178(1994).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1380, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for the proper melanization and sclerotization of
CC the cuticle. {ECO:0000269|PubMed:12393882, ECO:0000269|PubMed:7568156,
CC ECO:0000269|PubMed:8000074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Releases C-terminal Arg and Lys from polypeptides.;
CC EC=3.4.17.22;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0 for carboxypeptidase domain 1, and 5.0-6.0 for
CC domain 2.;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=B, 1B long tail-1;
CC IsoId=P42787-1; Sequence=Displayed;
CC Name=2; Synonyms=C;
CC IsoId=P42787-2; Sequence=VSP_037495;
CC Name=3; Synonyms=1A long tail-1, D;
CC IsoId=P42787-3; Sequence=VSP_000773;
CC Name=4; Synonyms=H;
CC IsoId=P42787-4; Sequence=VSP_000773, VSP_000779;
CC Name=5; Synonyms=1B long tail-2, G;
CC IsoId=P42787-5; Sequence=VSP_000779;
CC Name=6; Synonyms=1A short, E;
CC IsoId=P42787-6; Sequence=VSP_000773, VSP_000775, VSP_000776;
CC Name=7; Synonyms=1B short, F;
CC IsoId=P42787-7; Sequence=VSP_000775, VSP_000776;
CC Name=8; Synonyms=G, I;
CC IsoId=P42787-8; Sequence=VSP_037495, VSP_000779;
CC -!- DEVELOPMENTAL STAGE: Embryonic and adult stages.
CC {ECO:0000269|PubMed:8000074}.
CC -!- DOMAIN: There are 3 carboxypeptidase-like domains. Only the first two
CC domains seem to have kept a catalytic activity.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA91650.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC46486.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF545816; AAN73045.1; -; mRNA.
DR EMBL; AF545817; AAN73046.1; -; mRNA.
DR EMBL; AF545818; AAN73047.1; -; mRNA.
DR EMBL; AF545819; AAN73048.1; -; mRNA.
DR EMBL; AF545820; AAN73049.1; -; mRNA.
DR EMBL; AE014298; AAF45514.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF45515.4; -; Genomic_DNA.
DR EMBL; AE014298; AAO41630.2; -; Genomic_DNA.
DR EMBL; AE014298; AAS65237.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65238.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65239.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65240.1; -; Genomic_DNA.
DR EMBL; AE014298; ACL82874.1; -; Genomic_DNA.
DR EMBL; AL009147; CAA15634.1; -; Genomic_DNA.
DR EMBL; AL009147; CAA15635.1; -; Genomic_DNA.
DR EMBL; BT029935; ABM92809.1; -; mRNA.
DR EMBL; BT099720; ACV53084.1; -; mRNA.
DR EMBL; BT100310; ACZ52622.1; -; mRNA.
DR EMBL; U29591; AAA91650.1; ALT_FRAME; mRNA.
DR EMBL; U29592; AAA91651.1; -; mRNA.
DR EMBL; U03883; AAC46486.1; ALT_SEQ; Genomic_DNA.
DR PIR; T13284; T13284.
DR PIR; T13420; T13420.
DR PIR; T13421; T13421.
DR RefSeq; NP_001138141.1; NM_001144669.2. [P42787-8]
DR RefSeq; NP_001284742.1; NM_001297813.1. [P42787-6]
DR RefSeq; NP_001284743.1; NM_001297814.1. [P42787-7]
DR RefSeq; NP_001284744.1; NM_001297815.1. [P42787-5]
DR RefSeq; NP_525032.2; NM_080293.4. [P42787-1]
DR RefSeq; NP_726675.3; NM_166846.5. [P42787-4]
DR RefSeq; NP_788852.2; NM_176679.3. [P42787-1]
DR RefSeq; NP_996319.1; NM_206596.2. [P42787-5]
DR RefSeq; NP_996320.1; NM_206597.2. [P42787-7]
DR RefSeq; NP_996321.1; NM_206598.3. [P42787-6]
DR RefSeq; NP_996322.1; NM_206599.2. [P42787-3]
DR AlphaFoldDB; P42787; -.
DR SMR; P42787; -.
DR BioGRID; 57568; 3.
DR IntAct; P42787; 2.
DR STRING; 7227.FBpp0089126; -.
DR MEROPS; M14.037; -.
DR MEROPS; M14.A20; -.
DR GlyGen; P42787; 11 sites.
DR iPTMnet; P42787; -.
DR PaxDb; P42787; -.
DR PRIDE; P42787; -.
DR DNASU; 30998; -.
DR EnsemblMetazoa; FBtr0070081; FBpp0070080; FBgn0004648. [P42787-1]
DR EnsemblMetazoa; FBtr0070084; FBpp0089123; FBgn0004648. [P42787-3]
DR EnsemblMetazoa; FBtr0070085; FBpp0089124; FBgn0004648. [P42787-6]
DR EnsemblMetazoa; FBtr0070086; FBpp0089125; FBgn0004648. [P42787-7]
DR EnsemblMetazoa; FBtr0070087; FBpp0089126; FBgn0004648. [P42787-5]
DR EnsemblMetazoa; FBtr0290016; FBpp0288455; FBgn0004648. [P42787-4]
DR EnsemblMetazoa; FBtr0290017; FBpp0288456; FBgn0004648. [P42787-8]
DR EnsemblMetazoa; FBtr0340146; FBpp0309132; FBgn0004648. [P42787-6]
DR EnsemblMetazoa; FBtr0344737; FBpp0311069; FBgn0004648. [P42787-7]
DR EnsemblMetazoa; FBtr0344738; FBpp0311070; FBgn0004648. [P42787-1]
DR EnsemblMetazoa; FBtr0344739; FBpp0311071; FBgn0004648. [P42787-5]
DR GeneID; 30998; -.
DR KEGG; dme:Dmel_CG4122; -.
DR CTD; 30998; -.
DR FlyBase; FBgn0004648; svr.
DR VEuPathDB; VectorBase:FBgn0004648; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000156919; -.
DR InParanoid; P42787; -.
DR OMA; YHEAKKM; -.
DR PhylomeDB; P42787; -.
DR BRENDA; 3.4.17.22; 1994.
DR Reactome; R-DME-977606; Regulation of Complement cascade.
DR SignaLink; P42787; -.
DR BioGRID-ORCS; 30998; 0 hits in 3 CRISPR screens.
DR ChiTaRS; svr; fly.
DR GenomeRNAi; 30998; -.
DR PRO; PR:P42787; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004648; Expressed in seminal fluid secreting gland and 24 other tissues.
DR ExpressionAtlas; P42787; baseline and differential.
DR Genevisible; P42787; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; HDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:FlyBase.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:FlyBase.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0061837; P:neuropeptide processing; IMP:FlyBase.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 2.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 2.
DR SUPFAM; SSF49464; SSF49464; 4.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Carboxypeptidase; Cuticle; Glycoprotein; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1406
FT /note="Carboxypeptidase D"
FT /id="PRO_0000004405"
FT TOPO_DOM 26..1312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1313..1333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1334..1406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 26..446
FT /note="Domain 1"
FT REGION 447..865
FT /note="Domain 2"
FT REGION 866..1313
FT /note="Domain 3"
FT MOTIF 1343..1345
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 305
FT /note="Proton donor/acceptor 1"
FT /evidence="ECO:0000250|UniProtKB:Q90240"
FT ACT_SITE 730
FT /note="Proton donor/acceptor 2"
FT /evidence="ECO:0000250|UniProtKB:Q90240"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 626
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT MOD_RES 1380
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT VAR_SEQ 1..152
FT /note="MPTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYASQEQLEDLFAG
FT LEKAYPNQAKVHFLGRSLEGRNLLALQISRNTRSRNLLTPPVKYIANMHGDETVGRQLL
FT VYMAQYLLGNHERISDLGQLVNSTDIYLVPTMNPDGYALSQ -> MLFFCLALIIGCAV
FT GEYSEVRVIQEEDNFLESPHYLKNEEIGDLFSQLAKDYPDLAQTYTIGKSLEDRPIYAL
FT ALSAPTGESKNGDLLRPMVKLVANIQGDEAVGRQMVLYMAEYLATHYDGDPKVQALLNL
FT TEIHFLPTCNPDGFAKAK (in isoform 3, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12393882"
FT /id="VSP_000773"
FT VAR_SEQ 2..152
FT /note="PTLGLLFASIGIAVLAMGVPHCRGYTIKEDESFLQQPHYASQEQLEDLFAGL
FT EKAYPNQAKVHFLGRSLEGRNLLALQISRNTRSRNLLTPPVKYIANMHGDETVGRQLLV
FT YMAQYLLGNHERISDLGQLVNSTDIYLVPTMNPDGYALSQ -> NTCL (in
FT isoform 2 and isoform 8)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_037495"
FT VAR_SEQ 426..435
FT /note="NFRKVKVERS -> ISSFYSPYYF (in isoform 6 and isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:12393882"
FT /id="VSP_000775"
FT VAR_SEQ 436..1406
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12393882"
FT /id="VSP_000776"
FT VAR_SEQ 1385..1406
FT /note="ELSQRAHLVNNQTNYSFIIQAA -> GMTIQPYFDEEQLERILHTDDDDDDG
FT PHMEPELDVADDSEDDIVMLHNNGNKRRH (in isoform 4, isoform 5 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:12393882, ECO:0000303|Ref.5"
FT /id="VSP_000779"
FT CONFLICT 733
FT /note="C -> Y (in Ref. 6; AAA91650)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041
FT /note="V -> E (in Ref. 5; ABM92809 and 6; AAA91650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1406 AA; 158789 MW; E7CF31AEC21363BD CRC64;
MPTLGLLFAS IGIAVLAMGV PHCRGYTIKE DESFLQQPHY ASQEQLEDLF AGLEKAYPNQ
AKVHFLGRSL EGRNLLALQI SRNTRSRNLL TPPVKYIANM HGDETVGRQL LVYMAQYLLG
NHERISDLGQ LVNSTDIYLV PTMNPDGYAL SQEGNCESLP NYVGRGNAAN IDLNRDFPDR
LEQSHVHQLR AQSRQPETAA LVNWIVSKPF VLSANFHGGA VVASYPYDNS LAHNECCEES
LTPDDRVFKQ LAHTYSDNHP IMRKGNNCND SFSGGITNGA HWYELSGGMQ DFNYAFSNCF
ELTIELSCCK YPAASTLPQE WQRNKASLLQ LLRQAHIGIK GLVTDASGFP IADANVYVAG
LEEKPMRTSK RGEYWRLLTP GLYSVHASAF GYQTSAPQQV RVTNDNQEAL RLDFKLAPVE
TNFDGNFRKV KVERSEPPQK LKKQFNGFLT PTKYEHHNFT AMESYLRAIS SSYPSLTRLY
SIGKSVQGRD LWVLEIFATP GSHVPGVPEF KYVANMHGNE VVGKELLLIL TKYMLERYGN
DDRITKLVNG TRMHFLYSMN PDGYEISIEG DRTGGVGRAN AHGIDLNRNF PDQYGTDRFN
KVTEPEVAAV MNWTLSLPFV LSANLHGGSL VANYPFDDNE NDFNDPFMRL RNSSINGRKP
NPTEDNALFK HLAGIYSNAH PTMYLGQPCE LFQNEFFPDG ITNGAQWYSV TGGMQDWNYV
RAGCLELTIE MGCDKFPKAA ELSRYWEDHR EPLLQFIEQV HCGIHGFVHS TIGTPIAGAV
VRLDGANHST YSQVFGDYWK LALPGRHNLT VLGDNYAPLR MEVEVPDVHP FEMRMDITLM
PDDPQHWASA NDFRIIENVV NTRYHTNPQV RARLAELENQ NGQIASFGYA DSEFGTIFNY
LKMTSDIGEP EEHKYKLLVV SSLYDTTAPL GREILLNLIR HLVEGFKLQD TSVVELLKRS
VIYFLPQTSK FQNVFDMYNS NTSICDPVLG DELAERILGP ETDQAKDVFL QFLRSERFDL
MLTFGAGNSD LNYPKGDSVL VKFAHRMQRT EFNYSPLQCP PSATRQLHRE TTERLTNMMY
RIYNLPVYTL GISCCRMPHQ KKIASVWRKN IDKIKNFLAL VKTGVSGLVQ NDKGQPLREA
YVRLLEHDRI INVTKNVARF QLMLPHGLYG LEVTAPNYES QMIKVDVEDG RVTELGIIRM
HPFTLIRGVV LELPNNDNRA TTSIAGVVLD ESNHPVRNAK VSVVGQTQLR NFTGSMGQYR
ISAVPLGTIT LKVEAPRHLE ATRQMHLIQG GLATENVVFH LKVNEHVFGL PRFLFILCAS
VLIIVGVIVC VLCAQFWFYR RHRGDKPYYN FSLLPQRGKE QFGLEDDDGG DDGETELFRS
PIKRELSQRA HLVNNQTNYS FIIQAA
