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Q05793

- PGBM_MOUSE

UniProt

Q05793 - PGBM_MOUSE

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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

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

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
Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_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: UniProtKB
  4. extracellular region Source: Reactome
  5. Golgi lumen Source: Reactome
  6. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

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 – 17745Combined sources
Beta strandi1779 – 17824Combined sources
Beta strandi1788 – 179912Combined sources
Beta strandi1802 – 18076Combined sources
Helixi1808 – 18103Combined sources
Beta strandi1817 – 18204Combined sources
Beta strandi1823 – 18264Combined sources
Helixi1831 – 18333Combined sources
Beta strandi1835 – 18428Combined sources
Beta strandi1847 – 185610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiQ05793.
KOiK06255.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
2.60.40.10. 15 hits.
4.10.400.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
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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        10         20         30         40         50
MGQRAVGSLL LGLLLHARLL AVTHGLRAYD GLSLPEDTET VTASRYGWTY
60 70 80 90 100
SYLSDDEDLL ADDASGDGLG SGDVGSGDFQ MVYFRALVNF TRSIEYSPQL
110 120 130 140 150
EDASAKEFRE VSEAVVEKLE PEYRKIPGDQ IVSVVFIKEL DGWVFVELDV
160 170 180 190 200
GSEGNADGSQ IQEVLHTVVS SGSIGPYVTS PWGFKFRRLG TVPQFPRVCT
210 220 230 240 250
ETEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVPE LSSSTPAVGK
260 270 280 290 300
VSPLPLWPEA ATTPPPPVTH GPQFLLPSVP GPSACGPQEA SCHSGHCIPR
310 320 330 340 350
DYLCDGQEDC RDGSDELGCA SPPPCEPNEF ACENGHCALK LWRCDGDFDC
360 370 380 390 400
EDRTDEANCS VKQPGEVCGP THFQCVSTNR CIPASFHCDE ESDCPDRSDE
410 420 430 440 450
FGCMPPQVVT PPQQSIQASR GQTVTFTCVA TGVPTPIINW RLNWGHIPAH
460 470 480 490 500
PRVTMTSEGG RGTLIIRDVK EADQGAYTCE AMNSRGMVFG IPDGVLELVP
510 520 530 540 550
QRGPCPDGHF YLEDSASCLP CFCFGVTNVC QSSLRFRDQI RLSFDQPNDF
560 570 580 590 600
KGVNVTMPSQ PGVPPLSSTQ LQIDPALQEF QLVDLSRRFL VHDAFWALPK
610 620 630 640 650
QFLGNKVDSY GGFLRYKVRY ELARGMLEPV QKPDVILVGA GYRLHSRGHT
660 670 680 690 700
PTHPGTLNQR QVQLSEEHWV HESGRPVQRA EMLQALASLE AVLLQTVYNT
710 720 730 740 750
KMASVGLSDI VMDTTVTHTT IHGRAHSVEE CRCPIGYSGL SCESCDAHFT
760 770 780 790 800
RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC LNCQHNTEGP QCDKCKPGFF
810 820 830 840 850
GDATKATATA CRPCPCPYID ASRRFSDTCF LDTDGQATCD ACAPGYTGRR
860 870 880 890 900
CESCAPGYEG NPIQPGGKCR PTTQEIVRCD ERGSLGTSGE TCRCKNNVVG
910 920 930 940 950
RLCNECSDGS FHLSKQNPDG CLKCFCMGVS RQCSSSSWSR AQVLGASEQP
960 970 980 990 1000
SQFSLSNAAG THTTSEGVSS PAPGELSFSS FHNLLSEPYF WSLPASFRGD
1010 1020 1030 1040 1050
KVTSYGGELR FTVMQRPRPS SAPLHRQPLV VLQGNNIVLE HHASRDPSPG
1060 1070 1080 1090 1100
QPSNFIVPFQ EQAWQRPDGQ PATREHLLMA LAGIDALLIQ ASYTQQPAES
1110 1120 1130 1140 1150
RLSGISMDVA VPENTGQDSA REVEQCTCPP GYRGPSCQDC DTGYTRVPSG
1160 1170 1180 1190 1200
LYLGTCERCN CHGHSETCEP ETGACQSCQH HTEGASCEQC QPGYYGDAQR
1210 1220 1230 1240 1250
GTPQDCQPCP CYGAPAAGQA AHTCFLDTDG HPTCDSCSPG HSGRHCERCA
1260 1270 1280 1290 1300
PGYYGNPSQG QPCHRDGQVP EVLGCGCDPH GSISSQCDAA GQCQCKAQVE
1310 1320 1330 1340 1350
GRSCSHCRPH HFHLSASNPE GCLPCFCMGV TQQCASSSYS RQLISTHFAP
1360 1370 1380 1390 1400
GDFQGFALVN PQRNSQLTGG FTVEPVHDGA RLSFSNFAHL GQESFYWQLP
1410 1420 1430 1440 1450
EIYQGDKVAA YGGKLRYTLS YTAGPQGSPL LDPDIQITGN NIMLVASQPA
1460 1470 1480 1490 1500
LQGPERRSYE IIFREEFWRR PDGQPATREH LLMALADLDE LLVRATFSSV
1510 1520 1530 1540 1550
PRAASISAVS LEGAQPGPSS GPRALEVEEC RCPPGYVGLS CQDCAPGYTR
1560 1570 1580 1590 1600
TGSGLYLGQC ELCECNGHSD LCHPETGACS RCQHNTAGEF CELCATGYYG
1610 1620 1630 1640 1650
DATAGTPEDC QPCACPLTNP ENMFSRTCES LGAGGYRCTA CEPGYTGQYC
1660 1670 1680 1690 1700
EQCAPGYEGD PNVQGGRCQP LTKESLEVQI HPSRSVVPQG GPHSLRCQVS
1710 1720 1730 1740 1750
GSPPHYFYWS REDGRPLPSS AQQRHQGSEL HFPSVQPSDA GVYICTCRNL
1760 1770 1780 1790 1800
IHTSNSRAEL LVAEAPSKPI MVTVEEQRSQ SVRPGADVTF ICTAKSKSPA
1810 1820 1830 1840 1850
YTLVWTRLHN GKLPSRAMDF NGILTIRNVQ PSDAGTYVCT GSNMFAMDQG
1860 1870 1880 1890 1900
TATLHVQVSG TSTAPVASIH PPQLTVQPGQ QAEFRCSATG NPTPMLEWIG
1910 1920 1930 1940 1950
GPSGQLPAKA QIHNGILRLP AIEPSDQGQY LCRALSSAGQ HVARAMLQVH
1960 1970 1980 1990 2000
GGSGPRVQVS PERTQVHEGR TVRLYCRAAG VPSASITWRK EGGSLPFRHQ
2010 2020 2030 2040 2050
AHGSRLRLHH MSVADSGEYV CRANNNIDAQ ETSIMISVSP STNSPPAPAS
2060 2070 2080 2090 2100
PAPIRIESSS SRVAEGQTLD LNCVVPGHAH AQVTWHKRGG SLPTHHQTHG
2110 2120 2130 2140 2150
SRLRLYQVSS ADSGEYVCSV LSSSGPLEAS VLVSITPAAA NVHIPGVVPP
2160 2170 2180 2190 2200
IRIETSSSRV AEGQTLDLSC VVPGQAHAQV TWHKRGGSLP AGHQVHGHML
2210 2220 2230 2240 2250
RLNRVSPADS GEYSCQVTGS SGTLEASVLV TIEASEPSPI PAPGLAQPVY
2260 2270 2280 2290 2300
IESSSSHLTE GQTVDLKCVV PGQAHAQVTW HKRGSSLPAR HQTHGSLLRL
2310 2320 2330 2340 2350
YQLSPADSGE YVCQVAGSSH PEHEASFKLT VPSSQNSSFR LRSPVISIEP
2360 2370 2380 2390 2400
PSSTVQQGQD ASFKCLIHEG AMPIKVEWKI RDQELEDNVH ISPNGSIITI
2410 2420 2430 2440 2450
VAPGPATMEP TACVASNVYG MAQSVVNLSV HGPPTVSVLP EGPVHVKMGK
2460 2470 2480 2490 2500
DITLECISSG EPRSSPRWTR LGIPVKLEPR MFGLMNSHAM LKIASVKPSD
2510 2520 2530 2540 2550
AGTYVCQAQN ALGTAQKQVE LIVDTGTVAP GTPQVQVEES ELTLEAGHTA
2560 2570 2580 2590 2600
TLHCSATGNP PPTIHWSKLR APLPWQHRIE GNTLVIPRVA QQDSGQYICN
2610 2620 2630 2640 2650
ATNSAGHTEA TVVLHVESPP YATIIPEHTS AQPGNLVQLQ CLAHGTPPLT
2660 2670 2680 2690 2700
YQWSLVGGVL PEKAVVRNQL LRLEPTVPED SGRYRCQVSN RVGSAEAFAQ
2710 2720 2730 2740 2750
VLVQGSSSNL PDTSIPGGST PTVQVTPQLE TRNIGASVEF HCAVPNERGT
2760 2770 2780 2790 2800
HLRWLKEGGQ LPPGHSVQDG VLRIQNLDQN CQGTYVCQAH GPWGQAQATA
2810 2820 2830 2840 2850
QLIVQALPSV LINVRTSVHS VVVGHSVEFE CLALGDPKPQ VTWSKVGGHL
2860 2870 2880 2890 2900
RPGIVQSGTI IRIAHVELAD AGQYRCAATN AAGTTQSHVL LLVQALPQIS
2910 2920 2930 2940 2950
TPPEIRVPAG SAAVFPCMAS GYPTPAITWS KVDGDLPPDS RLENNMLMLP
2960 2970 2980 2990 3000
SVRPEDAGTY VCTATNRQGK VKAFAYLQVP ERVIPYFTQT PYSFLPLPTI
3010 3020 3030 3040 3050
KDAYRKFEIK ITFRPDSADG MLLYNGQKRS PTNLANRQPD FISFGLVGGR
3060 3070 3080 3090 3100
PEFRFDAGSG MATIRHPTPL ALGQFHTVTL LRSLTQGSLI VGNLAPVNGT
3110 3120 3130 3140 3150
SQGKFQGLDL NEELYLGGYP DYGAIPKAGL SSGFVGCVRE LRIQGEEIVF
3160 3170 3180 3190 3200
HDVNLTTHGI SHCPTCQDRP CQNGGQCQDS ESSSYTCVCP AGFTAAAVNI
3210 3220 3230 3240 3250
RKPCTATPSL WADATCVNRP DGRGYTCRCH LGRSGVRCEE GVTVTTPSMS
3260 3270 3280 3290 3300
GAGSYLALPA LTNTHHELRL DVEFKPLEPN GILLFSGGKS GPVEDFVSLA
3310 3320 3330 3340 3350
MVGGHLEFRY ELGSGLAVLR SHEPLALGRW HRVSAERLNK DGSLRVDGGR
3360 3370 3380 3390 3400
PVLRSSPGKS QGLNLHTLLY LGGVEPSVQL SPATNMSAHF HGCVGEVSVN
3410 3420 3430 3440 3450
GKRLDLTYSF LGSQGVGQCY DSSPCERQPC RNGATCMPAG EYEFQCLCQD
3460 3470 3480 3490 3500
GFKGDLCEHE ENPCQLHEPC LNGGTCRGAR CLCLPGFSGP RCQQGAGYGV
3510 3520 3530 3540 3550
VESDWHPEGS GGNDAPGQYG AYFYDNGFLG LPGNSFSRSL PEVPETIEFE
3560 3570 3580 3590 3600
VRTSTADGLL LWQGVVREAS RSKDFISLGL QDGHLVFSYQ LGSGEARLVS
3610 3620 3630 3640 3650
GDPINDGEWH RITALREGQR GSIQVDGEDL VTGRSPGPNV AVNTKDIIYI
3660 3670 3680 3690 3700
GGAPDVATLT RGKFSSGITG CIKNLVLHTA RPGAPPPQPL DLQHRAQAGA

NTRPCPS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi Q05793.
KOi K06255.

Enzyme and pathway databases

Reactomei REACT_198654. HS-GAG biosynthesis.
REACT_202342. Laminin interactions.

Miscellaneous databases

ChiTaRSi Hspg2. mouse.
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 IPR013320. ConA-like_dom.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 151 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