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Q05793

- PGBM_MOUSE

UniProt

Q05793 - PGBM_MOUSE

Protein

Basement membrane-specific heparan sulfate proteoglycan core protein

Gene

Hspg2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development By similarity.By similarity
    Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6 By similarity.By similarity
    The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei3513 – 35142Cleavage; by BMP1By similarity
    Metal bindingi3574 – 35741CalciumBy similarity
    Metal bindingi3591 – 35911Calcium; via carbonyl oxygenBy similarity
    Metal bindingi3641 – 36411Calcium; via carbonyl oxygenBy similarity
    Metal bindingi3643 – 36431CalciumBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protease binding Source: BHF-UCL
    3. protein binding Source: BHF-UCL

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. brain development Source: MGI
    3. cardiac muscle tissue development Source: MGI
    4. cartilage development involved in endochondral bone morphogenesis Source: MGI
    5. chondrocyte differentiation Source: MGI
    6. embryonic skeletal system morphogenesis Source: MGI
    7. endochondral ossification Source: MGI
    8. extracellular matrix organization Source: MGI
    9. protein localization Source: MGI

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196607. Non-integrin membrane-ECM interactions.
    REACT_198654. HS-GAG biosynthesis.
    REACT_202342. Laminin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Basement membrane-specific heparan sulfate proteoglycan core protein
    Short name:
    HSPG
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Hspg2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:96257. Hspg2.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: MGI
    2. basement membrane Source: MGI
    3. extracellular matrix Source: MGI
    4. extracellular region Source: Reactome
    5. Golgi lumen Source: Reactome
    6. proteinaceous extracellular matrix Source: MGI

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    About 40% of perlecan null mice die at embryonic day 10.5, the rest die just after birth. Embryonic percelan-null mice exhibit cardiac abnormalities including mechanical instability in the early stages of development (E10.5) with lower amounts of critical basement membrane components, collagen IV and lamanins. Basement membranes are absent in cardiomyocytes whereas adherens junctions formed and matured around E9.5. Also have skeletal dysplasia characterized by micromelia with broad and bowed long bones, narrow thorax and craniofacial abnormalities. Cartilage matrix containd reduced and disorganized collagen fibrils and glycosaminoglycans. In cartilage, proliferation of chondrocytes was reduced and the prehypertrophic zone was diminished.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 37073686Basement membrane-specific heparan sulfate proteoglycan core proteinPRO_0000026697Add
    BLAST
    Chaini3008 – 3707700EndorepellinPRO_0000391623Add
    BLAST
    Chaini3514 – 3707194LG3 peptideBy similarityPRO_0000391624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi65 – 651O-linked (Xyl...) (heparan sulfate)Sequence Analysis
    Glycosylationi71 – 711O-linked (Xyl...) (heparan sulfate)Sequence Analysis
    Glycosylationi76 – 761O-linked (Xyl...) (heparan sulfate)Sequence Analysis
    Glycosylationi89 – 891N-linked (GlcNAc...)1 Publication
    Disulfide bondi199 ↔ 212By similarity
    Disulfide bondi206 ↔ 225By similarity
    Disulfide bondi219 ↔ 234By similarity
    Disulfide bondi285 ↔ 297By similarity
    Disulfide bondi292 ↔ 310By similarity
    Disulfide bondi304 ↔ 319By similarity
    Disulfide bondi325 ↔ 337By similarity
    Disulfide bondi332 ↔ 350By similarity
    Disulfide bondi344 ↔ 359By similarity
    Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi368 ↔ 381By similarity
    Disulfide bondi375 ↔ 394By similarity
    Disulfide bondi388 ↔ 403By similarity
    Disulfide bondi428 ↔ 479By similarity
    Glycosylationi554 – 5541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi764 ↔ 773By similarity
    Disulfide bondi766 ↔ 780By similarity
    Disulfide bondi783 ↔ 792By similarity
    Disulfide bondi795 ↔ 811By similarity
    Disulfide bondi814 ↔ 829By similarity
    Disulfide bondi816 ↔ 839By similarity
    Disulfide bondi842 ↔ 851By similarity
    Disulfide bondi854 ↔ 869By similarity
    Disulfide bondi879 ↔ 892By similarity
    Disulfide bondi894 ↔ 903By similarity
    Disulfide bondi906 ↔ 921By similarity
    Disulfide bondi1159 ↔ 1168By similarity
    Disulfide bondi1161 ↔ 1175By similarity
    Disulfide bondi1178 ↔ 1187By similarity
    Disulfide bondi1190 ↔ 1206By similarity
    Disulfide bondi1209 ↔ 1224By similarity
    Disulfide bondi1211 ↔ 1234By similarity
    Disulfide bondi1237 ↔ 1246By similarity
    Disulfide bondi1249 ↔ 1263By similarity
    Glycosylationi1256 – 12561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1275 ↔ 1287By similarity
    Disulfide bondi1277 ↔ 1293By similarity
    Disulfide bondi1295 ↔ 1304By similarity
    Disulfide bondi1307 ↔ 1322By similarity
    Disulfide bondi1563 ↔ 1572By similarity
    Disulfide bondi1565 ↔ 1579By similarity
    Disulfide bondi1582 ↔ 1591By similarity
    Disulfide bondi1594 ↔ 1610By similarity
    Disulfide bondi1613 ↔ 1628By similarity
    Disulfide bondi1615 ↔ 1638By similarity
    Disulfide bondi1641 ↔ 1650By similarity
    Disulfide bondi1653 ↔ 1668By similarity
    Disulfide bondi1792 ↔ 1839
    Disulfide bondi1886 ↔ 1932By similarity
    Glycosylationi1891 – 18911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1976 ↔ 2021By similarity
    Disulfide bondi2073 ↔ 2118By similarity
    Disulfide bondi2170 ↔ 2215By similarity
    Disulfide bondi2268 ↔ 2313By similarity
    Glycosylationi2336 – 23361N-linked (GlcNAc...)2 Publications
    Disulfide bondi2365 ↔ 2413By similarity
    Glycosylationi2394 – 23941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2427 – 24271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2456 ↔ 2506By similarity
    Disulfide bondi2554 ↔ 2599By similarity
    Glycosylationi2600 – 26001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2641 ↔ 2686By similarity
    Disulfide bondi2831 ↔ 2876By similarity
    Disulfide bondi2917 ↔ 2962By similarity
    Glycosylationi3098 – 30981N-linked (GlcNAc...)2 Publications
    Disulfide bondi3137 ↔ 3163By similarity
    Glycosylationi3154 – 31541N-linked (GlcNAc...)1 Publication
    Disulfide bondi3166 ↔ 3177By similarity
    Disulfide bondi3171 ↔ 3187By similarity
    Disulfide bondi3204 ↔ 3216By similarity
    Disulfide bondi3229 ↔ 3238By similarity
    Glycosylationi3385 – 33851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3393 ↔ 3419By similarity
    Disulfide bondi3425 ↔ 3436By similarity
    Disulfide bondi3430 ↔ 3446By similarity
    Disulfide bondi3448 ↔ 3457By similarity
    Disulfide bondi3464 ↔ 3476By similarity
    Disulfide bondi3470 ↔ 3481By similarity
    Disulfide bondi3483 ↔ 3492By similarity
    Disulfide bondi3671 ↔ 3705By similarity

    Post-translational modificationi

    Proteolytic processing produces the C-terminal angiogenic peptide, endorepellin. This peptide can be further processed to produce the LG3 peptide By similarity.By similarity
    N- and O-glycosylated; contains 3 heparan sulfate chains. The LG3 peptide contains at least three and up to five potential O-glycosylation sites and no N-glycosylation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Heparan sulfate, Proteoglycan

    Proteomic databases

    MaxQBiQ05793.
    PaxDbiQ05793.
    PRIDEiQ05793.

    PTM databases

    PhosphoSiteiQ05793.

    Expressioni

    Tissue specificityi

    Found in the basement membranes.

    Gene expression databases

    CleanExiMM_HSPG2.
    GenevestigatoriQ05793.

    Interactioni

    Subunit structurei

    Purified perlecan has a strong tendency to aggregate in dimers or stellate structures. It interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1 (via C-terminus) By similarity.By similarity

    Protein-protein interaction databases

    BioGridi200461. 2 interactions.
    IntActiQ05793. 4 interactions.
    MINTiMINT-215413.

    Structurei

    Secondary structure

    1
    3707
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1770 – 17745
    Beta strandi1779 – 17824
    Beta strandi1788 – 179912
    Beta strandi1802 – 18076
    Helixi1808 – 18103
    Beta strandi1817 – 18204
    Beta strandi1823 – 18264
    Helixi1831 – 18333
    Beta strandi1835 – 18428
    Beta strandi1847 – 185610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GL4X-ray2.00B1765-1858[»]
    ProteinModelPortaliQ05793.
    SMRiQ05793. Positions 1769-1857, 3514-3707.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05793.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 191112SEAPROSITE-ProRule annotationAdd
    BLAST
    Domaini195 – 23440LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini281 – 31939LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini320 – 35940LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini360 – 40344LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini404 – 504101Ig-like C2-type 1Add
    BLAST
    Domaini521 – 53010Laminin EGF-like 1; first partPROSITE-ProRule annotation
    Domaini538 – 730193Laminin IV type A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini731 – 76333Laminin EGF-like 1; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini764 – 81350Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini814 – 87158Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini879 – 92345Laminin EGF-like 4; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini924 – 93310Laminin EGF-like 5; first partPROSITE-ProRule annotation
    Domaini941 – 1125185Laminin IV type A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1126 – 115833Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1159 – 120850Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1209 – 126557Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1275 – 132450Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1325 – 133410Laminin EGF-like 9; first partPROSITE-ProRule annotation
    Domaini1344 – 1529186Laminin IV type A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1530 – 156233Laminin EGF-like 9; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1563 – 161250Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1613 – 167058Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1677 – 177195Ig-like C2-type 2Add
    BLAST
    Domaini1772 – 186594Ig-like C2-type 3Add
    BLAST
    Domaini1866 – 195489Ig-like C2-type 4Add
    BLAST
    Domaini1955 – 204995Ig-like C2-type 5Add
    BLAST
    Domaini2050 – 214899Ig-like C2-type 6Add
    BLAST
    Domaini2149 – 224496Ig-like C2-type 7Add
    BLAST
    Domaini2245 – 234399Ig-like C2-type 8Add
    BLAST
    Domaini2344 – 243693Ig-like C2-type 9Add
    BLAST
    Domaini2437 – 253296Ig-like C2-type 10Add
    BLAST
    Domaini2533 – 261987Ig-like C2-type 11Add
    BLAST
    Domaini2620 – 2720101Ig-like C2-type 12Add
    BLAST
    Domaini2721 – 280989Ig-like C2-type 13Add
    BLAST
    Domaini2810 – 289586Ig-like C2-type 14Add
    BLAST
    Domaini2896 – 298085Ig-like C2-type 15Add
    BLAST
    Domaini2984 – 3162179Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini3163 – 324179EGF-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini3245 – 3425181Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3518 – 3705188Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni3615 – 36173Mediates motor neuron attachmentSequence Analysis

    Sequence similaritiesi

    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 11 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 3 laminin G-like domains.PROSITE-ProRule annotation
    Contains 3 laminin IV type A domains.PROSITE-ProRule annotation
    Contains 4 LDL-receptor class A domains.PROSITE-ProRule annotation
    Contains 1 SEA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Immunoglobulin domain, Laminin EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG258321.
    HOGENOMiHOG000049276.
    HOVERGENiHBG008174.
    KOiK06255.

    Family and domain databases

    Gene3Di2.60.120.200. 3 hits.
    2.60.40.10. 15 hits.
    4.10.400.10. 4 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    IPR001791. Laminin_G.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR000082. SEA_dom.
    [Graphical view]
    PfamiPF00008. EGF. 1 hit.
    PF07679. I-set. 11 hits.
    PF00052. Laminin_B. 3 hits.
    PF00053. Laminin_EGF. 9 hits.
    PF00054. Laminin_G_1. 2 hits.
    PF02210. Laminin_G_2. 1 hit.
    PF00057. Ldl_recept_a. 4 hits.
    [Graphical view]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00181. EGF. 3 hits.
    SM00180. EGF_Lam. 7 hits.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 14 hits.
    SM00281. LamB. 3 hits.
    SM00282. LamG. 3 hits.
    SM00192. LDLa. 4 hits.
    SM00200. SEA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 4 hits.
    SSF57424. SSF57424. 4 hits.
    PROSITEiPS00022. EGF_1. 8 hits.
    PS01186. EGF_2. 5 hits.
    PS50026. EGF_3. 4 hits.
    PS01248. EGF_LAM_1. 11 hits.
    PS50027. EGF_LAM_2. 8 hits.
    PS50835. IG_LIKE. 15 hits.
    PS50025. LAM_G_DOMAIN. 3 hits.
    PS51115. LAMININ_IVA. 3 hits.
    PS01209. LDLRA_1. 4 hits.
    PS50068. LDLRA_2. 4 hits.
    PS50024. SEA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q05793-1 [UniParc]FASTAAdd to Basket

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    MGQRAVGSLL LGLLLHARLL AVTHGLRAYD GLSLPEDTET VTASRYGWTY     50
    SYLSDDEDLL ADDASGDGLG SGDVGSGDFQ MVYFRALVNF TRSIEYSPQL 100
    EDASAKEFRE VSEAVVEKLE PEYRKIPGDQ IVSVVFIKEL DGWVFVELDV 150
    GSEGNADGSQ IQEVLHTVVS SGSIGPYVTS PWGFKFRRLG TVPQFPRVCT 200
    ETEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVPE LSSSTPAVGK 250
    VSPLPLWPEA ATTPPPPVTH GPQFLLPSVP GPSACGPQEA SCHSGHCIPR 300
    DYLCDGQEDC RDGSDELGCA SPPPCEPNEF ACENGHCALK LWRCDGDFDC 350
    EDRTDEANCS VKQPGEVCGP THFQCVSTNR CIPASFHCDE ESDCPDRSDE 400
    FGCMPPQVVT PPQQSIQASR GQTVTFTCVA TGVPTPIINW RLNWGHIPAH 450
    PRVTMTSEGG RGTLIIRDVK EADQGAYTCE AMNSRGMVFG IPDGVLELVP 500
    QRGPCPDGHF YLEDSASCLP CFCFGVTNVC QSSLRFRDQI RLSFDQPNDF 550
    KGVNVTMPSQ PGVPPLSSTQ LQIDPALQEF QLVDLSRRFL VHDAFWALPK 600
    QFLGNKVDSY GGFLRYKVRY ELARGMLEPV QKPDVILVGA GYRLHSRGHT 650
    PTHPGTLNQR QVQLSEEHWV HESGRPVQRA EMLQALASLE AVLLQTVYNT 700
    KMASVGLSDI VMDTTVTHTT IHGRAHSVEE CRCPIGYSGL SCESCDAHFT 750
    RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC LNCQHNTEGP QCDKCKPGFF 800
    GDATKATATA CRPCPCPYID ASRRFSDTCF LDTDGQATCD ACAPGYTGRR 850
    CESCAPGYEG NPIQPGGKCR PTTQEIVRCD ERGSLGTSGE TCRCKNNVVG 900
    RLCNECSDGS FHLSKQNPDG CLKCFCMGVS RQCSSSSWSR AQVLGASEQP 950
    SQFSLSNAAG THTTSEGVSS PAPGELSFSS FHNLLSEPYF WSLPASFRGD 1000
    KVTSYGGELR FTVMQRPRPS SAPLHRQPLV VLQGNNIVLE HHASRDPSPG 1050
    QPSNFIVPFQ EQAWQRPDGQ PATREHLLMA LAGIDALLIQ ASYTQQPAES 1100
    RLSGISMDVA VPENTGQDSA REVEQCTCPP GYRGPSCQDC DTGYTRVPSG 1150
    LYLGTCERCN CHGHSETCEP ETGACQSCQH HTEGASCEQC QPGYYGDAQR 1200
    GTPQDCQPCP CYGAPAAGQA AHTCFLDTDG HPTCDSCSPG HSGRHCERCA 1250
    PGYYGNPSQG QPCHRDGQVP EVLGCGCDPH GSISSQCDAA GQCQCKAQVE 1300
    GRSCSHCRPH HFHLSASNPE GCLPCFCMGV TQQCASSSYS RQLISTHFAP 1350
    GDFQGFALVN PQRNSQLTGG FTVEPVHDGA RLSFSNFAHL GQESFYWQLP 1400
    EIYQGDKVAA YGGKLRYTLS YTAGPQGSPL LDPDIQITGN NIMLVASQPA 1450
    LQGPERRSYE IIFREEFWRR PDGQPATREH LLMALADLDE LLVRATFSSV 1500
    PRAASISAVS LEGAQPGPSS GPRALEVEEC RCPPGYVGLS CQDCAPGYTR 1550
    TGSGLYLGQC ELCECNGHSD LCHPETGACS RCQHNTAGEF CELCATGYYG 1600
    DATAGTPEDC QPCACPLTNP ENMFSRTCES LGAGGYRCTA CEPGYTGQYC 1650
    EQCAPGYEGD PNVQGGRCQP LTKESLEVQI HPSRSVVPQG GPHSLRCQVS 1700
    GSPPHYFYWS REDGRPLPSS AQQRHQGSEL HFPSVQPSDA GVYICTCRNL 1750
    IHTSNSRAEL LVAEAPSKPI MVTVEEQRSQ SVRPGADVTF ICTAKSKSPA 1800
    YTLVWTRLHN GKLPSRAMDF NGILTIRNVQ PSDAGTYVCT GSNMFAMDQG 1850
    TATLHVQVSG TSTAPVASIH PPQLTVQPGQ QAEFRCSATG NPTPMLEWIG 1900
    GPSGQLPAKA QIHNGILRLP AIEPSDQGQY LCRALSSAGQ HVARAMLQVH 1950
    GGSGPRVQVS PERTQVHEGR TVRLYCRAAG VPSASITWRK EGGSLPFRHQ 2000
    AHGSRLRLHH MSVADSGEYV CRANNNIDAQ ETSIMISVSP STNSPPAPAS 2050
    PAPIRIESSS SRVAEGQTLD LNCVVPGHAH AQVTWHKRGG SLPTHHQTHG 2100
    SRLRLYQVSS ADSGEYVCSV LSSSGPLEAS VLVSITPAAA NVHIPGVVPP 2150
    IRIETSSSRV AEGQTLDLSC VVPGQAHAQV TWHKRGGSLP AGHQVHGHML 2200
    RLNRVSPADS GEYSCQVTGS SGTLEASVLV TIEASEPSPI PAPGLAQPVY 2250
    IESSSSHLTE GQTVDLKCVV PGQAHAQVTW HKRGSSLPAR HQTHGSLLRL 2300
    YQLSPADSGE YVCQVAGSSH PEHEASFKLT VPSSQNSSFR LRSPVISIEP 2350
    PSSTVQQGQD ASFKCLIHEG AMPIKVEWKI RDQELEDNVH ISPNGSIITI 2400
    VAPGPATMEP TACVASNVYG MAQSVVNLSV HGPPTVSVLP EGPVHVKMGK 2450
    DITLECISSG EPRSSPRWTR LGIPVKLEPR MFGLMNSHAM LKIASVKPSD 2500
    AGTYVCQAQN ALGTAQKQVE LIVDTGTVAP GTPQVQVEES ELTLEAGHTA 2550
    TLHCSATGNP PPTIHWSKLR APLPWQHRIE GNTLVIPRVA QQDSGQYICN 2600
    ATNSAGHTEA TVVLHVESPP YATIIPEHTS AQPGNLVQLQ CLAHGTPPLT 2650
    YQWSLVGGVL PEKAVVRNQL LRLEPTVPED SGRYRCQVSN RVGSAEAFAQ 2700
    VLVQGSSSNL PDTSIPGGST PTVQVTPQLE TRNIGASVEF HCAVPNERGT 2750
    HLRWLKEGGQ LPPGHSVQDG VLRIQNLDQN CQGTYVCQAH GPWGQAQATA 2800
    QLIVQALPSV LINVRTSVHS VVVGHSVEFE CLALGDPKPQ VTWSKVGGHL 2850
    RPGIVQSGTI IRIAHVELAD AGQYRCAATN AAGTTQSHVL LLVQALPQIS 2900
    TPPEIRVPAG SAAVFPCMAS GYPTPAITWS KVDGDLPPDS RLENNMLMLP 2950
    SVRPEDAGTY VCTATNRQGK VKAFAYLQVP ERVIPYFTQT PYSFLPLPTI 3000
    KDAYRKFEIK ITFRPDSADG MLLYNGQKRS PTNLANRQPD FISFGLVGGR 3050
    PEFRFDAGSG MATIRHPTPL ALGQFHTVTL LRSLTQGSLI VGNLAPVNGT 3100
    SQGKFQGLDL NEELYLGGYP DYGAIPKAGL SSGFVGCVRE LRIQGEEIVF 3150
    HDVNLTTHGI SHCPTCQDRP CQNGGQCQDS ESSSYTCVCP AGFTAAAVNI 3200
    RKPCTATPSL WADATCVNRP DGRGYTCRCH LGRSGVRCEE GVTVTTPSMS 3250
    GAGSYLALPA LTNTHHELRL DVEFKPLEPN GILLFSGGKS GPVEDFVSLA 3300
    MVGGHLEFRY ELGSGLAVLR SHEPLALGRW HRVSAERLNK DGSLRVDGGR 3350
    PVLRSSPGKS QGLNLHTLLY LGGVEPSVQL SPATNMSAHF HGCVGEVSVN 3400
    GKRLDLTYSF LGSQGVGQCY DSSPCERQPC RNGATCMPAG EYEFQCLCQD 3450
    GFKGDLCEHE ENPCQLHEPC LNGGTCRGAR CLCLPGFSGP RCQQGAGYGV 3500
    VESDWHPEGS GGNDAPGQYG AYFYDNGFLG LPGNSFSRSL PEVPETIEFE 3550
    VRTSTADGLL LWQGVVREAS RSKDFISLGL QDGHLVFSYQ LGSGEARLVS 3600
    GDPINDGEWH RITALREGQR GSIQVDGEDL VTGRSPGPNV AVNTKDIIYI 3650
    GGAPDVATLT RGKFSSGITG CIKNLVLHTA RPGAPPPQPL DLQHRAQAGA 3700
    NTRPCPS 3707
    Length:3,707
    Mass (Da):398,294
    Last modified:November 1, 1995 - v1
    Checksum:iD41D2A2EBA65C80B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1192 – 11921P → T AA sequence (PubMed:2972708)Curated
    Sequence conflicti1227 – 12271D → L AA sequence (PubMed:2972708)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77174 mRNA. Translation: AAA39911.1.
    J04054 mRNA. Translation: AAA39899.1.
    J04055 mRNA. Translation: AAA39912.1.
    PIRiS18252.
    RefSeqiNP_032331.2. NM_008305.3.
    UniGeneiMm.273662.

    Genome annotation databases

    GeneIDi15530.
    KEGGimmu:15530.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77174 mRNA. Translation: AAA39911.1 .
    J04054 mRNA. Translation: AAA39899.1 .
    J04055 mRNA. Translation: AAA39912.1 .
    PIRi S18252.
    RefSeqi NP_032331.2. NM_008305.3.
    UniGenei Mm.273662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GL4 X-ray 2.00 B 1765-1858 [» ]
    ProteinModelPortali Q05793.
    SMRi Q05793. Positions 1769-1857, 3514-3707.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200461. 2 interactions.
    IntActi Q05793. 4 interactions.
    MINTi MINT-215413.

    PTM databases

    PhosphoSitei Q05793.

    Proteomic databases

    MaxQBi Q05793.
    PaxDbi Q05793.
    PRIDEi Q05793.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 15530.
    KEGGi mmu:15530.

    Organism-specific databases

    CTDi 3339.
    MGIi MGI:96257. Hspg2.

    Phylogenomic databases

    eggNOGi NOG258321.
    HOGENOMi HOG000049276.
    HOVERGENi HBG008174.
    KOi K06255.

    Enzyme and pathway databases

    Reactomei REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_198654. HS-GAG biosynthesis.
    REACT_202342. Laminin interactions.

    Miscellaneous databases

    EvolutionaryTracei Q05793.
    NextBioi 288458.
    PROi Q05793.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_HSPG2.
    Genevestigatori Q05793.

    Family and domain databases

    Gene3Di 2.60.120.200. 3 hits.
    2.60.40.10. 15 hits.
    4.10.400.10. 4 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    IPR001791. Laminin_G.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR000082. SEA_dom.
    [Graphical view ]
    Pfami PF00008. EGF. 1 hit.
    PF07679. I-set. 11 hits.
    PF00052. Laminin_B. 3 hits.
    PF00053. Laminin_EGF. 9 hits.
    PF00054. Laminin_G_1. 2 hits.
    PF02210. Laminin_G_2. 1 hit.
    PF00057. Ldl_recept_a. 4 hits.
    [Graphical view ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00181. EGF. 3 hits.
    SM00180. EGF_Lam. 7 hits.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 14 hits.
    SM00281. LamB. 3 hits.
    SM00282. LamG. 3 hits.
    SM00192. LDLa. 4 hits.
    SM00200. SEA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 4 hits.
    SSF57424. SSF57424. 4 hits.
    PROSITEi PS00022. EGF_1. 8 hits.
    PS01186. EGF_2. 5 hits.
    PS50026. EGF_3. 4 hits.
    PS01248. EGF_LAM_1. 11 hits.
    PS50027. EGF_LAM_2. 8 hits.
    PS50835. IG_LIKE. 15 hits.
    PS50025. LAM_G_DOMAIN. 3 hits.
    PS51115. LAMININ_IVA. 3 hits.
    PS01209. LDLRA_1. 4 hits.
    PS50068. LDLRA_2. 4 hits.
    PS50024. SEA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule."
      Noonan D.M., Fulle A., Valente P., Cai S., Horigan E., Sasaki M., Yamada Y., Hassell J.R.
      J. Biol. Chem. 266:22939-22947(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Melanoma.
    2. "Identification of cDNA clones encoding different domains of the basement membrane heparan sulfate proteoglycan."
      Noonan D.M., Horigan E.A., Ledbetter S.R., Vogeli G., Sasaki M., Yamada Y., Hassell J.R.
      J. Biol. Chem. 263:16379-16387(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 940-1601 AND 1870-2600, PARTIAL PROTEIN SEQUENCE.
    3. "Structural properties of recombinant domain III-3 of perlecan containing a globular domain inserted into an epidermal-growth-factor-like motif."
      Schulze B., Mann K., Battistutta R., Wiedemann H., Timpl R.
      Eur. J. Biochem. 231:551-556(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    4. "Perlecan is essential for cartilage and cephalic development."
      Arikawa-Hirasawa E., Watanabe H., Takami H., Hassell J.R., Yamada Y.
      Nat. Genet. 23:354-358(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    5. "BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan."
      Gonzalez E.M., Reed C.C., Bix G., Fu J., Zhang Y., Gopalakrishnan B., Greenspan D.S., Iozzo R.V.
      J. Biol. Chem. 280:7080-7087(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    6. "WARP is a novel multimeric component of the chondrocyte pericellular matrix that interacts with perlecan."
      Allen J.M., Bateman J.F., Hansen U., Wilson R., Bruckner P., Owens R.T., Sasaki T., Timpl R., Fitzgerald J.
      J. Biol. Chem. 281:7341-7349(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VWA1.
    7. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    8. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-89; ASN-2336; ASN-3098 AND ASN-3154.
      Tissue: Myoblast.
    9. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2336 AND ASN-3098.
    10. "Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1."
      Hopf M., Gohring W., Ries A., Timpl R., Hohenester E.
      Nat. Struct. Biol. 8:634-640(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1761-1858 IN COMPLEX WITH A NIDOGEN FRAGMENT.

    Entry informationi

    Entry nameiPGBM_MOUSE
    AccessioniPrimary (citable) accession number: Q05793
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3