APLP1_HUMAN
ID APLP1_HUMAN Reviewed; 650 AA.
AC P51693; O00113; Q96A92;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Amyloid beta precursor like protein 1 {ECO:0000312|HGNC:HGNC:597};
DE AltName: Full=Amyloid beta (A4) precursor-like protein 1 {ECO:0000250|UniProtKB:Q03157};
DE AltName: Full=Amyloid-like protein 1 {ECO:0000312|HGNC:HGNC:597};
DE Short=APLP {ECO:0000312|HGNC:HGNC:597};
DE Short=APLP-1;
DE Contains:
DE RecName: Full=C30;
DE Flags: Precursor;
GN Name=APLP1;
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] (ISOFORM 1).
RX PubMed=9428684; DOI=10.1111/j.1432-1033.1997.0354a.x;
RA Paliga K., Peraus G., Kreger S., Duwrrwang U., Hesse L., Multhaup G.,
RA Masters C.L., Beyreuther K., Weidemann A.;
RT "Human amyloid precursor-like protein 1 -- cDNA cloning, ectopic expression
RT in COS-7 cells and identification of soluble forms in the cerebrospinal
RT fluid.";
RL Eur. J. Biochem. 250:354-363(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9521588; DOI=10.1007/s004390050676;
RA Lenkkeri U., Kestila M., Lamerdin J.E., McCready P., Adamson A., Olsen A.,
RA Tryggvason K.;
RT "Structure of the human amyloid-precursor-like protein gene APLP1 at
RT 19q13.1.";
RL Hum. Genet. 102:192-196(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Ovary;
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 [5]
RP POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7494461; DOI=10.1016/0169-328x(95)00328-p;
RA Kim T.-W., Wu K., Xu J.-L., McAuliffe G., Tanzi R.E., Wasco W., Black I.B.;
RT "Selective localization of amyloid precursor-like protein 1 in the cerebral
RT cortex postsynaptic density.";
RL Brain Res. Mol. Brain Res. 32:36-44(1995).
RN [6]
RP HEPARIN AND ZINC-BINDING.
RX PubMed=7929392; DOI=10.1016/s0021-9258(18)47062-7;
RA Bush A.I., Pettingell W.H. Jr., de Paradis M., Tanzi R.E., Wasco W.;
RT "The amyloid beta-protein precursor and its mammalian homologues. Evidence
RT for a zinc-modulated heparin-binding superfamily.";
RL J. Biol. Chem. 269:26618-26621(1994).
RN [7]
RP INTERACTION WITH APBA2.
RX PubMed=9890987; DOI=10.1074/jbc.274.4.2243;
RA Tomita S., Ozaki T., Taru H., Oguchi S., Takeda S., Yagi Y., Sakiyama S.,
RA Kirino Y., Suzuki T.;
RT "Interaction of a neuron-specific protein containing PDZ domains with
RT Alzheimer's amyloid precursor protein.";
RL J. Biol. Chem. 274:2243-2254(1999).
RN [8]
RP EXTRACELLULAR COPPER-BINDING.
RX PubMed=12135352; DOI=10.1021/bi0258647;
RA Simons A., Ruppert T., Schmidt C., Schlicksupp A., Pipkorn R., Reed J.,
RA Masters C.L., White A.R., Cappai R., Beyreuther K., Bayer T.A.,
RA Multhaup G.;
RT "Evidence for a copper-binding superfamily of the amyloid precursor
RT protein.";
RL Biochemistry 41:9310-9320(2002).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-215; SER-227 AND THR-228, AND
RP STRUCTURE 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 [10]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 285-499, HEPARIN-BINDING,
RP MUTAGENESIS OF HIS-426; ARG-429 AND HIS-433, AND SUBUNIT.
RX PubMed=21574595; DOI=10.1021/bi101846x;
RA Lee S., Xue Y., Hu J., Wang Y., Liu X., Demeler B., Ha Y.;
RT "The E2 Domains of APP and APLP1 Share a Conserved Mode of Dimerization.";
RL Biochemistry 50:5453-5464(2011).
CC -!- FUNCTION: May play a role in postsynaptic function. The C-terminal
CC gamma-secretase processed fragment, ALID1, activates transcription
CC activation through APBB1 (Fe65) binding (By similarity). Couples to JIP
CC signal transduction through C-terminal binding. May interact with
CC cellular G-protein signaling pathways. Can regulate neurite outgrowth
CC through binding to components of the extracellular matrix such as
CC heparin and collagen I. {ECO:0000250}.
CC -!- FUNCTION: The gamma-CTF peptide, C30, is a potent enhancer of neuronal
CC apoptosis. {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer. Heparin binding promotes
CC homodimerization. Binds, via its C-terminus, to the PID domain of
CC several cytoplasmic proteins, including APBB and APBA family members,
CC MAPK8IP1 and DAB1 (By similarity). Binding to Dab1 inhibits its serine
CC phosphorylation (By similarity). Interacts with CPEB1. Interacts (via
CC NPXY motif) with DAB2 (via PID domain); the interaction is impaired by
CC tyrosine phosphorylation of the NPXY motif. Interacts (via NPXY motif)
CC with DAB1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P51693; P51693: APLP1; NbExp=4; IntAct=EBI-74648, EBI-74648;
CC P51693; Q06481: APLP2; NbExp=2; IntAct=EBI-74648, EBI-79306;
CC P51693; P05067-4: APP; NbExp=2; IntAct=EBI-74648, EBI-302641;
CC P51693; Q93074: MED12; NbExp=2; IntAct=EBI-74648, EBI-394357;
CC P51693; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-74648, EBI-11141397;
CC P51693; P17028: ZNF24; NbExp=2; IntAct=EBI-74648, EBI-707773;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [C30]: Cytoplasm. Note=C-terminally processed in
CC the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51693-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51693-2; Sequence=VSP_039100;
CC -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex where it is
CC localized to the postsynaptic density (PSD).
CC {ECO:0000269|PubMed:7494461}.
CC -!- DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated
CC proteins is required for the specific binding of the PID domain.
CC However, additional amino acids either N- or C-terminal to the NPXY
CC motif are often required for complete interaction. The NPXY site is
CC also involved in clathrin-mediated endocytosis.
CC -!- PTM: Proteolytically cleaved by caspases during neuronal apoptosis.
CC Cleaved, in vitro, at Asp-620 by caspase-3 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated. O-glycosylation with core 1 or possibly
CC core 8 glycans. Glycosylation on Ser-227 is the preferred site to Thr-
CC 228. {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23234360}.
CC -!- MISCELLANEOUS: Binds zinc and copper in the extracellular domain. Zinc-
CC binding increases heparin binding. No Cu(2+) reducing activity with
CC copper-binding.
CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01217}.
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DR EMBL; U48437; AAB96331.1; -; mRNA.
DR EMBL; AD000864; AAB50173.1; -; Genomic_DNA.
DR EMBL; BC012889; AAH12889.1; -; mRNA.
DR EMBL; BC013850; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS32997.1; -. [P51693-2]
DR RefSeq; NP_001019978.1; NM_001024807.2. [P51693-2]
DR RefSeq; NP_005157.1; NM_005166.4. [P51693-1]
DR PDB; 3PMR; X-ray; 2.11 A; A/B=285-499.
DR PDB; 3Q7G; X-ray; 2.30 A; A/B=285-494.
DR PDB; 3Q7L; X-ray; 2.20 A; A/B=285-494.
DR PDB; 3QMK; X-ray; 2.21 A; A/B=285-494.
DR PDB; 4RD9; X-ray; 2.60 A; A/B=292-494.
DR PDB; 4RDA; X-ray; 2.50 A; A/B=290-495.
DR PDBsum; 3PMR; -.
DR PDBsum; 3Q7G; -.
DR PDBsum; 3Q7L; -.
DR PDBsum; 3QMK; -.
DR PDBsum; 4RD9; -.
DR PDBsum; 4RDA; -.
DR AlphaFoldDB; P51693; -.
DR SMR; P51693; -.
DR BioGRID; 106830; 52.
DR DIP; DIP-30846N; -.
DR IntAct; P51693; 48.
DR MINT; P51693; -.
DR STRING; 9606.ENSP00000221891; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 716; 1 O-Linked glycan (1 site).
DR GlyGen; P51693; 7 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P51693; -.
DR PhosphoSitePlus; P51693; -.
DR BioMuta; APLP1; -.
DR DMDM; 28558769; -.
DR MassIVE; P51693; -.
DR PaxDb; P51693; -.
DR PeptideAtlas; P51693; -.
DR PRIDE; P51693; -.
DR ProteomicsDB; 56379; -. [P51693-1]
DR ProteomicsDB; 56380; -. [P51693-2]
DR TopDownProteomics; P51693-2; -. [P51693-2]
DR Antibodypedia; 16162; 266 antibodies from 28 providers.
DR DNASU; 333; -.
DR Ensembl; ENST00000221891.9; ENSP00000221891.4; ENSG00000105290.13. [P51693-2]
DR Ensembl; ENST00000652533.1; ENSP00000498366.1; ENSG00000105290.13. [P51693-1]
DR GeneID; 333; -.
DR KEGG; hsa:333; -.
DR MANE-Select; ENST00000221891.9; ENSP00000221891.4; NM_001024807.3; NP_001019978.1. [P51693-2]
DR UCSC; uc002ocf.4; human. [P51693-1]
DR CTD; 333; -.
DR DisGeNET; 333; -.
DR GeneCards; APLP1; -.
DR HGNC; HGNC:597; APLP1.
DR HPA; ENSG00000105290; Tissue enriched (brain).
DR MIM; 104775; gene.
DR neXtProt; NX_P51693; -.
DR OpenTargets; ENSG00000105290; -.
DR PharmGKB; PA24884; -.
DR VEuPathDB; HostDB:ENSG00000105290; -.
DR eggNOG; KOG3540; Eukaryota.
DR GeneTree; ENSGT00530000063252; -.
DR InParanoid; P51693; -.
DR OMA; CKSYVYW; -.
DR OrthoDB; 953529at2759; -.
DR PhylomeDB; P51693; -.
DR TreeFam; TF317274; -.
DR PathwayCommons; P51693; -.
DR SignaLink; P51693; -.
DR BioGRID-ORCS; 333; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; APLP1; human.
DR EvolutionaryTrace; P51693; -.
DR GeneWiki; APLP1; -.
DR GenomeRNAi; 333; -.
DR Pharos; P51693; Tbio.
DR PRO; PR:P51693; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P51693; protein.
DR Bgee; ENSG00000105290; Expressed in C1 segment of cervical spinal cord and 137 other tissues.
DR ExpressionAtlas; P51693; baseline and differential.
DR Genevisible; P51693; HS.
DR GO; GO:0005604; C:basement membrane; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0031694; F:alpha-2A adrenergic receptor binding; IPI:BHF-UCL.
DR GO; GO:0031695; F:alpha-2B adrenergic receptor binding; IPI:BHF-UCL.
DR GO; GO:0031696; F:alpha-2C adrenergic receptor binding; IPI:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071874; P:cellular response to norepinephrine stimulus; IDA:BHF-UCL.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; ISS:ARUK-UCL.
DR GO; GO:0030900; P:forebrain development; ISS:ARUK-UCL.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:Ensembl.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
DR Gene3D; 1.20.120.770; -; 1.
DR Gene3D; 3.30.1490.140; -; 1.
DR Gene3D; 3.90.570.10; -; 1.
DR InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR InterPro; IPR008155; Amyloid_glyco.
DR InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR InterPro; IPR008154; Amyloid_glyco_extra.
DR InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR InterPro; IPR019543; APP_amyloid_C.
DR InterPro; IPR019744; APP_CUBD_CS.
DR InterPro; IPR036176; E2_sf.
DR PANTHER; PTHR23103; PTHR23103; 1.
DR Pfam; PF10515; APP_amyloid; 1.
DR Pfam; PF12924; APP_Cu_bd; 1.
DR Pfam; PF12925; APP_E2; 1.
DR Pfam; PF02177; APP_N; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR SMART; SM00006; A4_EXTRA; 1.
DR SUPFAM; SSF109843; SSF109843; 1.
DR SUPFAM; SSF56491; SSF56491; 1.
DR SUPFAM; SSF89811; SSF89811; 1.
DR PROSITE; PS00319; APP_CUBD; 1.
DR PROSITE; PS51869; APP_E1; 1.
DR PROSITE; PS51870; APP_E2; 1.
DR PROSITE; PS00320; APP_INTRA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell adhesion;
KW Cell membrane; Copper; Cytoplasm; Disulfide bond; Endocytosis;
KW Glycoprotein; Heparin-binding; Membrane; Metal-binding; Neurodegeneration;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..650
FT /note="Amyloid beta precursor like protein 1"
FT /id="PRO_0000000203"
FT PEPTIDE 621..650
FT /note="C30"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000204"
FT TOPO_DOM 39..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 50..212
FT /note="E1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DOMAIN 293..484
FT /note="E2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01218"
FT REGION 50..146
FT /note="GFLD subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT REGION 154..212
FT /note="CuBD subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT REGION 214..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..305
FT /note="O-glycosylated at three sites"
FT REGION 310..342
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 410..441
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 442..459
FT /note="Collagen-binding"
FT /evidence="ECO:0000250"
FT REGION 492..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..649
FT /note="Interaction with DAB1"
FT /evidence="ECO:0000250"
FT REGION 636..650
FT /note="Interaction with DAB2"
FT /evidence="ECO:0000250"
FT MOTIF 604..615
FT /note="Basolateral sorting signal"
FT /evidence="ECO:0000250"
FT MOTIF 640..643
FT /note="Clathrin-binding"
FT /evidence="ECO:0000255"
FT MOTIF 640..643
FT /note="NPXY motif; contains endocytosis signal"
FT COMPBIAS 531..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 561
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT SITE 620..621
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT CARBOHYD 215
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19838169"
FT CARBOHYD 227
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000305|PubMed:19838169"
FT CARBOHYD 228
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:19838169"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 95..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 120..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 156..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 167..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 181..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT VAR_SEQ 517
FT /note="D -> DA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039100"
FT MUTAGEN 426
FT /note="H->A: Reduced affinity for heparin. Reduces
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:21574595"
FT MUTAGEN 429
FT /note="R->A: Strongly reduced affinity for heparin.
FT Strongly reduced homodimerization."
FT /evidence="ECO:0000269|PubMed:21574595"
FT MUTAGEN 433
FT /note="H->A: Reduced affinity for heparin. Reduces
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:21574595"
FT CONFLICT 48
FT /note="A -> P (in Ref. 1; AAB96331)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="P -> S (in Ref. 4; BC013850)"
FT /evidence="ECO:0000305"
FT HELIX 293..298
FT /evidence="ECO:0007829|PDB:3PMR"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4RDA"
FT HELIX 306..337
FT /evidence="ECO:0007829|PDB:3PMR"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:3PMR"
FT HELIX 344..399
FT /evidence="ECO:0007829|PDB:3PMR"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:3PMR"
FT HELIX 406..437
FT /evidence="ECO:0007829|PDB:3PMR"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:3PMR"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:3PMR"
FT HELIX 446..467
FT /evidence="ECO:0007829|PDB:3PMR"
FT HELIX 471..485
FT /evidence="ECO:0007829|PDB:3PMR"
SQ SEQUENCE 650 AA; 72176 MW; B95F0F4D1C5CBAC7 CRC64;
MGPASPAARG LSRRPGQPPL PLLLPLLLLL LRAQPAIGSL AGGSPGAAEA PGSAQVAGLC
GRLTLHRDLR TGRWEPDPQR SRRCLRDPQR VLEYCRQMYP ELQIARVEQA TQAIPMERWC
GGSRSGSCAH PHHQVVPFRC LPGEFVSEAL LVPEGCRFLH QERMDQCESS TRRHQEAQEA
CSSQGLILHG SGMLLPCGSD RFRGVEYVCC PPPGTPDPSG TAVGDPSTRS WPPGSRVEGA
EDEEEEESFP QPVDDYFVEP PQAEEEEETV PPPSSHTLAV VGKVTPTPRP TDGVDIYFGM
PGEISEHEGF LRAKMDLEER RMRQINEVMR EWAMADNQSK NLPKADRQAL NEHFQSILQT
LEEQVSGERQ RLVETHATRV IALINDQRRA ALEGFLAALQ ADPPQAERVL LALRRYLRAE
QKEQRHTLRH YQHVAAVDPE KAQQMRFQVH THLQVIEERV NQSLGLLDQN PHLAQELRPQ
IQELLHSEHL GPSELEAPAP GGSSEDKGGL QPPDSKDDTP MTLPKGSTEQ DAASPEKEKM
NPLEQYERKV NASVPRGFPF HSSEIQRDEL APAGTGVSRE AVSGLLIMGA GGGSLIVLSM
LLLRRKKPYG AISHGVVEVD PMLTLEEQQL RELQRHGYEN PTYRFLEERP
