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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.2 Publications
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.2 Publications
The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity By similarity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei3513 – 35142Cleavage; by BMP1 By similarity
Metal bindingi3574 – 35741Calcium By similarity
Metal bindingi3591 – 35911Calcium; via carbonyl oxygen By similarity
Metal bindingi3641 – 36411Calcium; via carbonyl oxygen By similarity
Metal bindingi3643 – 36431Calcium By similarity

GO - Molecular functioni

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

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_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. Golgi lumen Source: Reactome
  2. basal lamina Source: MGI
  3. basement membrane Source: MGI
  4. extracellular matrix Source: MGI
  5. extracellular region 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 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 37073686Basement membrane-specific heparan sulfate proteoglycan core protein
PRO_0000026697Add
BLAST
Chaini3008 – 3707700Endorepellin
PRO_0000391623Add
BLAST
Chaini3514 – 3707194LG3 peptide By similarity
PRO_0000391624Add
BLAST

Amino acid modifications

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

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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ05793.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3615 – 36173Mediates motor neuron attachment Reviewed prediction

Sequence similaritiesi

Contains 1 EGF-like domain.
Contains 1 SEA domain.

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

« Hide

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1192 – 11921P → T AA sequence 1 Publication
Sequence conflicti1227 – 12271D → L AA sequence 1 Publication

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
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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...

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

« 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: September 3, 2014
This is version 148 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

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