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Database: UniProt
Entry: A0A3B3SE98_9TELE
LinkDB: A0A3B3SE98_9TELE
Original site: A0A3B3SE98_9TELE 
ID   A0A3B3SE98_9TELE        Unreviewed;      3450 AA.
AC   A0A3B3SE98;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Heparan sulfate proteoglycan 2 {ECO:0000313|Ensembl:ENSPKIP00000029082.1};
GN   Name=HSPG2 {ECO:0000313|Ensembl:ENSPKIP00000029082.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000029082.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000029082.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   Ensembl; ENSPKIT00000009872.1; ENSPKIP00000029082.1; ENSPKIG00000009289.1.
DR   GeneTree; ENSGT00940000156670; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   GO; GO:0072359; P:circulatory system development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00055; EGF_Lam; 6.
DR   CDD; cd05743; Ig_Perlecan_like; 1.
DR   CDD; cd05754; IgI_Perlecan_like; 1.
DR   CDD; cd00110; LamG; 3.
DR   CDD; cd00112; LDLa; 4.
DR   Gene3D; 2.60.120.200; -; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 12.
DR   Gene3D; 2.10.25.10; Laminin; 9.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR12231:SF267; BASEMENT MEMBRANE-SPECIFIC HEPARAN SULFATE PROTEOGLYCAN CORE PROTEIN; 1.
DR   PANTHER; PTHR12231; CTX-RELATED TYPE I TRANSMEMBRANE PROTEIN; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07679; I-set; 5.
DR   Pfam; PF13927; Ig_3; 7.
DR   Pfam; PF00052; Laminin_B; 3.
DR   Pfam; PF00053; Laminin_EGF; 7.
DR   Pfam; PF00054; Laminin_G_1; 3.
DR   Pfam; PF00057; Ldl_recept_a; 4.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 11.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00180; EGF_Lam; 6.
DR   SMART; SM00409; IG; 12.
DR   SMART; SM00408; IGc2; 12.
DR   SMART; SM00406; IGv; 5.
DR   SMART; SM00281; LamB; 3.
DR   SMART; SM00282; LamG; 3.
DR   SMART; SM00192; LDLa; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 6.
DR   SUPFAM; SSF48726; Immunoglobulin; 13.
DR   SUPFAM; SSF57424; LDL receptor-like module; 4.
DR   PROSITE; PS00022; EGF_1; 4.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01248; EGF_LAM_1; 4.
DR   PROSITE; PS50027; EGF_LAM_2; 4.
DR   PROSITE; PS50835; IG_LIKE; 13.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR   PROSITE; PS51115; LAMININ_IVA; 3.
DR   PROSITE; PS01209; LDLRA_1; 3.
DR   PROSITE; PS50068; LDLRA_2; 4.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          337..414
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          477..662
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          696..745
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          746..803
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          875..1052
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1086..1135
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1242..1461
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1495..1544
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1587..1695
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1701..1787
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1816..1899
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1910..2021
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2029..2113
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2124..2207
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2215..2303
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2311..2385
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2401..2483
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2487..2525
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2539..2623
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2628..2704
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2716..2899
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2895..2932
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2935..2973
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2979..3159
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3155..3192
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3194..3227
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          3252..3448
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   COILED          1961..1988
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        164..176
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        171..189
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        183..198
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        216..228
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        223..241
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        235..250
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        256..268
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        263..281
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        275..290
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        319..334
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        715..724
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        774..783
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1105..1114
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1514..1523
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2922..2931
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2944..2961
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2963..2972
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3182..3191
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        3217..3226
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   3450 AA;  377290 MW;  CD2D4AAE007FB18A CRC64;
     SFLRPSYLFN IKVTVSLTRR AEIHLEGSVA VCLHFVRVTM RCCTCLTTPP PLPPIPVYYR
     ALVNFTNSFV YGPELEDINS PLFKEITDAV VDTVPDPHGP LLFRKLGNNV FVELDVGSEV
     NMNTEQIRNV LFSVVKEGSI ASYITSVHGF QFRRLGVDDN RQPCTDSEFT CRDGECIPSE
     YRCDKRHDCR DMSDESDCVL AGPRPPVLKP PVLRPCRADQ ATCQNGQCIP RDYLCDGERD
     CSDGSDELAC GTPSPCEPNE FKCQNGHCAL KLWRCDGDND CGDNSDESYC PVKSPGDTCA
     PEQFVCVRDR TCIPASYQCD EEPDCPDRSD EIGCTPPTIT SPPEESVMAM RGETVTFTCK
     AVGVPTPIIT WRLNWGHIPN SSRISMASVN GHGTLTIQDV KDGDQGAYTC EAINAKGMVF
     GIPDGVLTVK PNTAGHCTGG HFGAGDGSAC IPCFCFGITK NCQNTGRHRN QIRLRFTEED
     NFKGVNVSFP SRPASPPLSS TQLLINTEVE EFQLVDLSRR FLSLESFWTL PSQFLGNKVD
     SYGGSLNYKV RFTLARGETE PVQKPDVVLV GNGQKLIYRR TSPTSPRITN EREIKFTEEN
     WQHASGRLVT REDLMMTLVN LESINIRTTY DNRMVSVALR DIVMDTTTVE FSGQGPANDV
     EQCRCPPGYS GLSCESCASG FERVSGGSYL GSCAGCNCNG HASACDPISG HCLSCQHNTE
     GPQCNKCRPG YFGDPTRGRS DDCKPCPCPY IETSRRFSDT CFLDSDSQAT CDACRPGYTG
     RRCEKCAPGY HGNPLQPNGK CVPQSECISC FTGLTFNRDS ALQSNVVGAL CDECRSSSFH
     LTEDNPDGCL QCFCMGVTKQ CTSSTWSRDQ VRGGVNGQLF SLANAAHTRT ISDGIGQRGG
     SEVIFRFSTH VPHDVLFWVL PESFRGDKVT AYGGELRYTV SYVPRQHSAP IEGQPDVVLQ
     GNGIMLEHYS STKPTPHVAT VITVPFRESE WKRSDRQPCT REHLLMALAD ITVFMIRATY
     ANSMTETGIA DIWMDIAVPH STGNERALEV EECACPQGYR GPSCQECDVG YIRTGSGLYL
     GTCERCNCHG YATTCDPDTG NCLQCQHNTA GPHCDRCRPG YYGNPRSGSP AACQPCPCPG
     TSPDIQFSRT CFLDSDGQPT CDGCPPGFTG RRCERHVLIT LYLPLLQAYV EGPLCAQCKP
     GHFHLSPAHK DGCLSCFCMG ITQQCSSSSY YRDLVSSSFA PGHFQGFALV NRQRTNRIAT
     GFTVEVSTQG TQLSFSRFGN LAQEAHYWQL PEAYRGDKVV CTGHVTRHYA LVYKGFSLYP
     EEVLFWQLPP QYKGVKVGSY GGRLKYTLSY VSDPRGSSIE DVDVQIIGND ITLVTRQPWP
     RGQGTRESRQ FEVVFKEENW QRPDGMPATR EHLMMVLADL DDILIRASYY TDMRSTSISD
     VSMEVAVPNY TGLTQALEVE ECRCPPGYRG LSCQDCAAGY TRTGGGLYLG HCELCDCNGH
     SDSCHPETGV CTSCLHNTMG QMCEQCAAGF FGDPTAGTPE DCQPCACPHT DPENQFSHTC
     ESTGNGGYQC TACQRGYTGQ YCERCSPGYV GNPQERIKCH IHSDAVSLVV RIQPERVQVS
     QGGSVTLRCQ VTSLPPHKFQ WSREDGRSLS SNAEIHRHGE ELHFSSVQPH DAGVYICTCQ
     DQHNTNRSRA EIVVTAVSTK PIEVTVEEPK TQSVRVGSTI HFICTAKSKS PAYTLVWTRQ
     GRGNLPDRAV DFNGILTIHN VQPEDAGIYV CTGSNMLAMD EGTAILHVPE PSQTQMFYTA
     YEMFEGHRLP ADGSQPVATV HPPVLSVQQG QRAEFRCTVT GNPPPVIEWI GGPGGRINRN
     AVIRGEVLSI PAVERADEAE YICKALNVHG EHAARAMLYV HSASPKSLLP QVQVSPQTVD
     IHEGETLRLY CRAGGTPTPG LDWKRREGPL PQQAIPSHGF HQFKSNSLDV LQKRIEELQA
     RMERTDIGTL LIPNIKASDA GTYLCVGTNS IGSSEASIKV KVIKADPIPT WITILPQVAT
     VQEGQWLDLS CVVPGNFPAS VTWRRTDRPL SSNHQVLLYI VLRILQASAD DAGEYTCRVQ
     GGPAHQQASV TVSVTSSTSR LQTPIISIEP HSTAVRLGEA ASFRCYIYSG AQPVHLEWKL
     AGNQPLPDNV KVGPDNSVIT ITNAQPRNQG PYHCVASNRF GITRSIASLI VKDSPKVTVT
     PKSPVRVWVG EPINLECQAR GDPRPSVSWH RMDNSHRIVL NSPVPMESNA VMQVLVARPE
     DSGTYICTAQ SSEGTSEARV EVIIEGGAQV PSFPIASVPE TFMVVKEGQT VTLHCNAQGY
     PTPTITWSKL RAPLPWRHSV VNNTLVLTSV GRQDSGQYIC NATNNLGVSE VLIMLDVETP
     PYATTLPDDL SVRVGEVIRL QCLSHGTPPL TFRWTKVNGS MSARAEVRGG NLQINLATAN
     DVGTYKCAVS NKVGSSEALA RVIVRSPLEV RVYPQVEVKA PGSAVEFTCS ANGGIQTTVE
     WLKEGGSLPA NHHIKDALPK VMINIRTSVQ TVMLGSSVEF ECHATGDPEP TVQWSKVDGT
     LFSHVVVKGG MLTINRVTEV DAGKYRCTAT NNVGSVQSEV ILNVQTLPQI TAQPEVREVT
     VGSTAVFPCM ASGYPLPQIT WTKLEGPLAP KASQEGHVLT IPNVTFEDSG TYVCTASNKQ
     GKVQAFSMLK VHERIMPYFT QTPLSYLTLP TIKNSYKAFN IKITFRPDNV DGVILYAGMI
     LYNGQKRTTG ADFISLGLVG GRPEFRFDVG SGMATIRFPT PIKLGEFHTV ELYRNTTQGA
     IIVDGQAPIN GSSQGKFQGL DLNEELHVGG YPNYSIVSKT TGLKNGFVGC IRQLIIQGDE
     VIFKDLDRSS TGVSNCPTCK DRPCQNGGVC QDSETSNYKC ECVRGFTGSN CEHHSSMHCH
     PEACGSDATC INNPSGRGYD CRCHLGKFGE KCMHGTLVTT PLFNGEDSFI TYPPLTNIHN
     DLRVDLEFKP MEANGLMFFS GGKKMKVEDF VSLAMVDNHI EFRYELGTGM AVLRSRDPVK
     LGQWHQIEAE RIDRDGSLKV DQAREVRRSS PGKAQGLNIY TPMYLGGVPS MDILPKPANI
     SMLFKGCIGE VSINGKKVDL SYSFTESQSI SQCVDANPCE RRPCRNGGTC LYSAEYEFQC
     LCQDGFEGEL CEVVKDTCQH NSECQNGGRC LANRCVCSSG FTGLFCETRH SLSFPDAMWD
     LEGSGGNDSP AEYAAYFHDN GYLALPKSVF PRSSLDAPEV IELEIRTASS EGLILWQGVV
     GLWAQENELG DQGKGKDFIS LGLQNGHLVF SYQLGSGEAK ITSKEPINNA DWHMVRAVRT
     GKQGYIQVDG GPISRGLSRG ESVMVNTKGD IYLGGAPNMV ALTGGKFSTG ITGCIRNLVL
     ANTLPWDRQL QPIDILAHSG EGINVERCSS
//
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