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Q05793 (PGBM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Basement membrane-specific heparan sulfate proteoglycan core protein
Short name=HSPG

Cleaved into the following 2 chains:

  1. Endorepellin
  2. LG3 peptide
Gene names
Name:Hspg2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length3707 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.7

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. Ref.4 Ref.7

The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity By similarity. Ref.4 Ref.7

Subunit structure

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. Ref.6

Subcellular location

Secreted › extracellular space › extracellular matrix › basement membrane.

Tissue specificity

Found in the basement membranes.

Post-translational modification

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.

Disruption phenotype

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. Ref.4 Ref.7

Sequence similarities

Contains 1 EGF-like domain.

Contains 15 Ig-like C2-type (immunoglobulin-like) domains.

Contains 11 laminin EGF-like domains.

Contains 3 laminin G-like domains.

Contains 3 laminin IV type A domains.

Contains 4 LDL-receptor class A domains.

Contains 1 SEA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 37073686Basement membrane-specific heparan sulfate proteoglycan core protein
PRO_0000026697
Chain3008 – 3707700Endorepellin
PRO_0000391623
Chain3514 – 3707194LG3 peptide By similarity
PRO_0000391624

Regions

Domain80 – 194115SEA
Domain195 – 23440LDL-receptor class A 1
Domain281 – 31939LDL-receptor class A 2
Domain320 – 35940LDL-receptor class A 3
Domain360 – 40344LDL-receptor class A 4
Domain404 – 504101Ig-like C2-type 1
Domain521 – 53010Laminin EGF-like 1; first part
Domain538 – 730193Laminin IV type A 1
Domain731 – 76333Laminin EGF-like 1; second part
Domain764 – 81350Laminin EGF-like 2
Domain814 – 87158Laminin EGF-like 3
Domain879 – 92345Laminin EGF-like 4; truncated
Domain924 – 93310Laminin EGF-like 5; first part
Domain941 – 1125185Laminin IV type A 2
Domain1126 – 115833Laminin EGF-like 5; second part
Domain1159 – 120850Laminin EGF-like 6
Domain1209 – 126557Laminin EGF-like 7
Domain1275 – 132450Laminin EGF-like 8
Domain1325 – 133410Laminin EGF-like 9; first part
Domain1344 – 1529186Laminin IV type A 3
Domain1530 – 156233Laminin EGF-like 9; second part
Domain1563 – 161250Laminin EGF-like 10
Domain1613 – 167058Laminin EGF-like 11
Domain1677 – 177195Ig-like C2-type 2
Domain1772 – 186594Ig-like C2-type 3
Domain1866 – 195489Ig-like C2-type 4
Domain1955 – 204995Ig-like C2-type 5
Domain2050 – 214899Ig-like C2-type 6
Domain2149 – 224496Ig-like C2-type 7
Domain2245 – 234399Ig-like C2-type 8
Domain2344 – 243693Ig-like C2-type 9
Domain2437 – 253296Ig-like C2-type 10
Domain2533 – 261987Ig-like C2-type 11
Domain2620 – 2720101Ig-like C2-type 12
Domain2721 – 280989Ig-like C2-type 13
Domain2810 – 289586Ig-like C2-type 14
Domain2896 – 298085Ig-like C2-type 15
Domain2984 – 3162179Laminin G-like 1
Domain3163 – 324179EGF-like
Domain3245 – 3425181Laminin G-like 2
Domain3518 – 3705188Laminin G-like 3
Region3615 – 36173Mediates motor neuron attachment Potential

Sites

Metal binding35741Calcium By similarity
Metal binding35911Calcium; via carbonyl oxygen By similarity
Metal binding36411Calcium; via carbonyl oxygen By similarity
Metal binding36431Calcium By similarity
Site3513 – 35142Cleavage; by BMP1 By similarity

Amino acid modifications

Glycosylation651O-linked (Xyl...) (heparan sulfate) Potential
Glycosylation711O-linked (Xyl...) (heparan sulfate) Potential
Glycosylation761O-linked (Xyl...) (heparan sulfate) Potential
Glycosylation891N-linked (GlcNAc...) Ref.8
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation5541N-linked (GlcNAc...) Potential
Glycosylation12561N-linked (GlcNAc...) Potential
Glycosylation18911N-linked (GlcNAc...) Potential
Glycosylation23361N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation23941N-linked (GlcNAc...) Potential
Glycosylation24271N-linked (GlcNAc...) Potential
Glycosylation26001N-linked (GlcNAc...) Potential
Glycosylation30981N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation31541N-linked (GlcNAc...) Ref.8
Glycosylation33851N-linked (GlcNAc...) Potential
Disulfide bond199 ↔ 212 By similarity
Disulfide bond206 ↔ 225 By similarity
Disulfide bond219 ↔ 234 By similarity
Disulfide bond285 ↔ 297 By similarity
Disulfide bond292 ↔ 310 By similarity
Disulfide bond304 ↔ 319 By similarity
Disulfide bond325 ↔ 337 By similarity
Disulfide bond332 ↔ 350 By similarity
Disulfide bond344 ↔ 359 By similarity
Disulfide bond368 ↔ 381 By similarity
Disulfide bond375 ↔ 394 By similarity
Disulfide bond388 ↔ 403 By similarity
Disulfide bond428 ↔ 479 By similarity
Disulfide bond764 ↔ 773 By similarity
Disulfide bond766 ↔ 780 By similarity
Disulfide bond783 ↔ 792 By similarity
Disulfide bond795 ↔ 811 By similarity
Disulfide bond814 ↔ 829 By similarity
Disulfide bond816 ↔ 839 By similarity
Disulfide bond842 ↔ 851 By similarity
Disulfide bond854 ↔ 869 By similarity
Disulfide bond879 ↔ 892 By similarity
Disulfide bond894 ↔ 903 By similarity
Disulfide bond906 ↔ 921 By similarity
Disulfide bond1159 ↔ 1168 By similarity
Disulfide bond1161 ↔ 1175 By similarity
Disulfide bond1178 ↔ 1187 By similarity
Disulfide bond1190 ↔ 1206 By similarity
Disulfide bond1209 ↔ 1224 By similarity
Disulfide bond1211 ↔ 1234 By similarity
Disulfide bond1237 ↔ 1246 By similarity
Disulfide bond1249 ↔ 1263 By similarity
Disulfide bond1275 ↔ 1287 By similarity
Disulfide bond1277 ↔ 1293 By similarity
Disulfide bond1295 ↔ 1304 By similarity
Disulfide bond1307 ↔ 1322 By similarity
Disulfide bond1563 ↔ 1572 By similarity
Disulfide bond1565 ↔ 1579 By similarity
Disulfide bond1582 ↔ 1591 By similarity
Disulfide bond1594 ↔ 1610 By similarity
Disulfide bond1613 ↔ 1628 By similarity
Disulfide bond1615 ↔ 1638 By similarity
Disulfide bond1641 ↔ 1650 By similarity
Disulfide bond1653 ↔ 1668 By similarity
Disulfide bond1792 ↔ 1839
Disulfide bond1886 ↔ 1932 By similarity
Disulfide bond1976 ↔ 2021 By similarity
Disulfide bond2073 ↔ 2118 By similarity
Disulfide bond2170 ↔ 2215 By similarity
Disulfide bond2268 ↔ 2313 By similarity
Disulfide bond2365 ↔ 2413 By similarity
Disulfide bond2456 ↔ 2506 By similarity
Disulfide bond2554 ↔ 2599 By similarity
Disulfide bond2641 ↔ 2686 By similarity
Disulfide bond2831 ↔ 2876 By similarity
Disulfide bond2917 ↔ 2962 By similarity
Disulfide bond3137 ↔ 3163 By similarity
Disulfide bond3166 ↔ 3177 By similarity
Disulfide bond3171 ↔ 3187 By similarity
Disulfide bond3204 ↔ 3216 By similarity
Disulfide bond3229 ↔ 3238 By similarity
Disulfide bond3393 ↔ 3419 By similarity
Disulfide bond3425 ↔ 3436 By similarity
Disulfide bond3430 ↔ 3446 By similarity
Disulfide bond3448 ↔ 3457 By similarity
Disulfide bond3464 ↔ 3476 By similarity
Disulfide bond3470 ↔ 3481 By similarity
Disulfide bond3483 ↔ 3492 By similarity
Disulfide bond3671 ↔ 3705 By similarity

Experimental info

Sequence conflict11921P → T AA sequence Ref.2
Sequence conflict12271D → L AA sequence Ref.2

Secondary structure

1 .................... 3707
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05793 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D41D2A2EBA65C80B

FASTA3,707398,294
        10         20         30         40         50         60 
MGQRAVGSLL LGLLLHARLL AVTHGLRAYD GLSLPEDTET VTASRYGWTY SYLSDDEDLL 

        70         80         90        100        110        120 
ADDASGDGLG SGDVGSGDFQ MVYFRALVNF TRSIEYSPQL EDASAKEFRE VSEAVVEKLE 

       130        140        150        160        170        180 
PEYRKIPGDQ IVSVVFIKEL DGWVFVELDV GSEGNADGSQ IQEVLHTVVS SGSIGPYVTS 

       190        200        210        220        230        240 
PWGFKFRRLG TVPQFPRVCT ETEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVPE 

       250        260        270        280        290        300 
LSSSTPAVGK VSPLPLWPEA ATTPPPPVTH GPQFLLPSVP GPSACGPQEA SCHSGHCIPR 

       310        320        330        340        350        360 
DYLCDGQEDC RDGSDELGCA SPPPCEPNEF ACENGHCALK LWRCDGDFDC EDRTDEANCS 

       370        380        390        400        410        420 
VKQPGEVCGP THFQCVSTNR CIPASFHCDE ESDCPDRSDE FGCMPPQVVT PPQQSIQASR 

       430        440        450        460        470        480 
GQTVTFTCVA TGVPTPIINW RLNWGHIPAH PRVTMTSEGG RGTLIIRDVK EADQGAYTCE 

       490        500        510        520        530        540 
AMNSRGMVFG IPDGVLELVP QRGPCPDGHF YLEDSASCLP CFCFGVTNVC QSSLRFRDQI 

       550        560        570        580        590        600 
RLSFDQPNDF KGVNVTMPSQ PGVPPLSSTQ LQIDPALQEF QLVDLSRRFL VHDAFWALPK 

       610        620        630        640        650        660 
QFLGNKVDSY GGFLRYKVRY ELARGMLEPV QKPDVILVGA GYRLHSRGHT PTHPGTLNQR 

       670        680        690        700        710        720 
QVQLSEEHWV HESGRPVQRA EMLQALASLE AVLLQTVYNT KMASVGLSDI VMDTTVTHTT 

       730        740        750        760        770        780 
IHGRAHSVEE CRCPIGYSGL SCESCDAHFT RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC 

       790        800        810        820        830        840 
LNCQHNTEGP QCDKCKPGFF GDATKATATA CRPCPCPYID ASRRFSDTCF LDTDGQATCD 

       850        860        870        880        890        900 
ACAPGYTGRR CESCAPGYEG NPIQPGGKCR PTTQEIVRCD ERGSLGTSGE TCRCKNNVVG 

       910        920        930        940        950        960 
RLCNECSDGS FHLSKQNPDG CLKCFCMGVS RQCSSSSWSR AQVLGASEQP SQFSLSNAAG 

       970        980        990       1000       1010       1020 
THTTSEGVSS PAPGELSFSS FHNLLSEPYF WSLPASFRGD KVTSYGGELR FTVMQRPRPS 

      1030       1040       1050       1060       1070       1080 
SAPLHRQPLV VLQGNNIVLE HHASRDPSPG QPSNFIVPFQ EQAWQRPDGQ PATREHLLMA 

      1090       1100       1110       1120       1130       1140 
LAGIDALLIQ ASYTQQPAES RLSGISMDVA VPENTGQDSA REVEQCTCPP GYRGPSCQDC 

      1150       1160       1170       1180       1190       1200 
DTGYTRVPSG LYLGTCERCN CHGHSETCEP ETGACQSCQH HTEGASCEQC QPGYYGDAQR 

      1210       1220       1230       1240       1250       1260 
GTPQDCQPCP CYGAPAAGQA AHTCFLDTDG HPTCDSCSPG HSGRHCERCA PGYYGNPSQG 

      1270       1280       1290       1300       1310       1320 
QPCHRDGQVP EVLGCGCDPH GSISSQCDAA GQCQCKAQVE GRSCSHCRPH HFHLSASNPE 

      1330       1340       1350       1360       1370       1380 
GCLPCFCMGV TQQCASSSYS RQLISTHFAP GDFQGFALVN PQRNSQLTGG FTVEPVHDGA 

      1390       1400       1410       1420       1430       1440 
RLSFSNFAHL GQESFYWQLP EIYQGDKVAA YGGKLRYTLS YTAGPQGSPL LDPDIQITGN 

      1450       1460       1470       1480       1490       1500 
NIMLVASQPA LQGPERRSYE IIFREEFWRR PDGQPATREH LLMALADLDE LLVRATFSSV 

      1510       1520       1530       1540       1550       1560 
PRAASISAVS LEGAQPGPSS GPRALEVEEC RCPPGYVGLS CQDCAPGYTR TGSGLYLGQC 

      1570       1580       1590       1600       1610       1620 
ELCECNGHSD LCHPETGACS RCQHNTAGEF CELCATGYYG DATAGTPEDC QPCACPLTNP 

      1630       1640       1650       1660       1670       1680 
ENMFSRTCES LGAGGYRCTA CEPGYTGQYC EQCAPGYEGD PNVQGGRCQP LTKESLEVQI 

      1690       1700       1710       1720       1730       1740 
HPSRSVVPQG GPHSLRCQVS GSPPHYFYWS REDGRPLPSS AQQRHQGSEL HFPSVQPSDA 

      1750       1760       1770       1780       1790       1800 
GVYICTCRNL IHTSNSRAEL LVAEAPSKPI MVTVEEQRSQ SVRPGADVTF ICTAKSKSPA 

      1810       1820       1830       1840       1850       1860 
YTLVWTRLHN GKLPSRAMDF NGILTIRNVQ PSDAGTYVCT GSNMFAMDQG TATLHVQVSG 

      1870       1880       1890       1900       1910       1920 
TSTAPVASIH PPQLTVQPGQ QAEFRCSATG NPTPMLEWIG GPSGQLPAKA QIHNGILRLP 

      1930       1940       1950       1960       1970       1980 
AIEPSDQGQY LCRALSSAGQ HVARAMLQVH GGSGPRVQVS PERTQVHEGR TVRLYCRAAG 

      1990       2000       2010       2020       2030       2040 
VPSASITWRK EGGSLPFRHQ AHGSRLRLHH MSVADSGEYV CRANNNIDAQ ETSIMISVSP 

      2050       2060       2070       2080       2090       2100 
STNSPPAPAS PAPIRIESSS SRVAEGQTLD LNCVVPGHAH AQVTWHKRGG SLPTHHQTHG 

      2110       2120       2130       2140       2150       2160 
SRLRLYQVSS ADSGEYVCSV LSSSGPLEAS VLVSITPAAA NVHIPGVVPP IRIETSSSRV 

      2170       2180       2190       2200       2210       2220 
AEGQTLDLSC VVPGQAHAQV TWHKRGGSLP AGHQVHGHML RLNRVSPADS GEYSCQVTGS 

      2230       2240       2250       2260       2270       2280 
SGTLEASVLV TIEASEPSPI PAPGLAQPVY IESSSSHLTE GQTVDLKCVV PGQAHAQVTW 

      2290       2300       2310       2320       2330       2340 
HKRGSSLPAR HQTHGSLLRL YQLSPADSGE YVCQVAGSSH PEHEASFKLT VPSSQNSSFR 

      2350       2360       2370       2380       2390       2400 
LRSPVISIEP PSSTVQQGQD ASFKCLIHEG AMPIKVEWKI RDQELEDNVH ISPNGSIITI 

      2410       2420       2430       2440       2450       2460 
VAPGPATMEP TACVASNVYG MAQSVVNLSV HGPPTVSVLP EGPVHVKMGK DITLECISSG 

      2470       2480       2490       2500       2510       2520 
EPRSSPRWTR LGIPVKLEPR MFGLMNSHAM LKIASVKPSD AGTYVCQAQN ALGTAQKQVE 

      2530       2540       2550       2560       2570       2580 
LIVDTGTVAP GTPQVQVEES ELTLEAGHTA TLHCSATGNP PPTIHWSKLR APLPWQHRIE 

      2590       2600       2610       2620       2630       2640 
GNTLVIPRVA QQDSGQYICN ATNSAGHTEA TVVLHVESPP YATIIPEHTS AQPGNLVQLQ 

      2650       2660       2670       2680       2690       2700 
CLAHGTPPLT YQWSLVGGVL PEKAVVRNQL LRLEPTVPED SGRYRCQVSN RVGSAEAFAQ 

      2710       2720       2730       2740       2750       2760 
VLVQGSSSNL PDTSIPGGST PTVQVTPQLE TRNIGASVEF HCAVPNERGT HLRWLKEGGQ 

      2770       2780       2790       2800       2810       2820 
LPPGHSVQDG VLRIQNLDQN CQGTYVCQAH GPWGQAQATA QLIVQALPSV LINVRTSVHS 

      2830       2840       2850       2860       2870       2880 
VVVGHSVEFE CLALGDPKPQ VTWSKVGGHL RPGIVQSGTI IRIAHVELAD AGQYRCAATN 

      2890       2900       2910       2920       2930       2940 
AAGTTQSHVL LLVQALPQIS TPPEIRVPAG SAAVFPCMAS GYPTPAITWS KVDGDLPPDS 

      2950       2960       2970       2980       2990       3000 
RLENNMLMLP SVRPEDAGTY VCTATNRQGK VKAFAYLQVP ERVIPYFTQT PYSFLPLPTI 

      3010       3020       3030       3040       3050       3060 
KDAYRKFEIK ITFRPDSADG MLLYNGQKRS PTNLANRQPD FISFGLVGGR PEFRFDAGSG 

      3070       3080       3090       3100       3110       3120 
MATIRHPTPL ALGQFHTVTL LRSLTQGSLI VGNLAPVNGT SQGKFQGLDL NEELYLGGYP 

      3130       3140       3150       3160       3170       3180 
DYGAIPKAGL SSGFVGCVRE LRIQGEEIVF HDVNLTTHGI SHCPTCQDRP CQNGGQCQDS 

      3190       3200       3210       3220       3230       3240 
ESSSYTCVCP AGFTAAAVNI RKPCTATPSL WADATCVNRP DGRGYTCRCH LGRSGVRCEE 

      3250       3260       3270       3280       3290       3300 
GVTVTTPSMS GAGSYLALPA LTNTHHELRL DVEFKPLEPN GILLFSGGKS GPVEDFVSLA 

      3310       3320       3330       3340       3350       3360 
MVGGHLEFRY ELGSGLAVLR SHEPLALGRW HRVSAERLNK DGSLRVDGGR PVLRSSPGKS 

      3370       3380       3390       3400       3410       3420 
QGLNLHTLLY LGGVEPSVQL SPATNMSAHF HGCVGEVSVN GKRLDLTYSF LGSQGVGQCY 

      3430       3440       3450       3460       3470       3480 
DSSPCERQPC RNGATCMPAG EYEFQCLCQD GFKGDLCEHE ENPCQLHEPC LNGGTCRGAR 

      3490       3500       3510       3520       3530       3540 
CLCLPGFSGP RCQQGAGYGV VESDWHPEGS GGNDAPGQYG AYFYDNGFLG LPGNSFSRSL 

      3550       3560       3570       3580       3590       3600 
PEVPETIEFE VRTSTADGLL LWQGVVREAS RSKDFISLGL QDGHLVFSYQ LGSGEARLVS 

      3610       3620       3630       3640       3650       3660 
GDPINDGEWH RITALREGQR GSIQVDGEDL VTGRSPGPNV AVNTKDIIYI GGAPDVATLT 

      3670       3680       3690       3700 
RGKFSSGITG CIKNLVLHTA RPGAPPPQPL DLQHRAQAGA NTRPCPS

« Hide

References

« Hide 'large scale' references
[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]"Perlecan is critical for heart stability."
Sasse P., Malan D., Fleischmann M., Roell W., Gustafsson E., Bostani T., Fan Y., Kolbe T., Breitbach M., Addicks K., Welz A., Brem G., Hescheler J., Aszodi A., Costell M., Bloch W., Fleischmann B.K.
Cardiovasc. Res. 80:435-444(2008) [PubMed] [Europe PMC] [Abstract]
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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M77174 mRNA. Translation: AAA39911.1.
J04054 mRNA. Translation: AAA39899.1.
J04055 mRNA. Translation: AAA39912.1.
IPIIPI00113824.
PIRS18252.
RefSeqNP_032331.2. NM_008305.3.
UniGeneMm.273662.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GL4X-ray2.00B1765-1858[»]
ProteinModelPortalQ05793.
SMRQ05793. Positions 196-486, 730-926, 1121-1327, 1516-3707.
ModBaseSearch...

Protein-protein interaction databases

IntActQ05793. 1 interaction.
MINTMINT-215413.

PTM databases

PhosphoSiteQ05793.

Proteomic databases

PaxDbQ05793.
PRIDEQ05793.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID15530.
KEGGmmu:15530.

Organism-specific databases

CTD3339.
MGIMGI:96257. Hspg2.

Phylogenomic databases

eggNOGNOG258321.
HOGENOMHOG000049276.
HOVERGENHBG008174.
KOK06255.

Enzyme and pathway databases

ReactomeREACT_112621. Metabolism.
REACT_118324. Disease.

Gene expression databases

CleanExMM_HSPG2.
GenevestigatorQ05793.
GermOnlineENSMUSG00000028763. Mus musculus.

Family and domain databases

Gene3D2.60.120.200. 3 hits.
2.60.40.10. 15 hits.
4.10.400.10. 4 hits.
InterProIPR008985. 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]
PfamPF00008. EGF. 1 hit.
PF07679. I-set. 12 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]
SMARTSM00181. 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]
SUPFAMSSF49899. ConA_like_lec_gl. 3 hits.
SSF57424. LDL_rcpt_classA_cys-rich. 4 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ05793.
NextBio288458.
SOURCESearch...

Entry information

Entry namePGBM_MOUSE
AccessionPrimary (citable) accession number: Q05793
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 29, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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