ID A0A1S3MHD3_SALSA Unreviewed; 3756 AA.
AC A0A1S3MHD3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein isoform X8 {ECO:0000313|RefSeq:XP_014002291.1};
GN Name=LOC100380784 {ECO:0000313|RefSeq:XP_014002291.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014002291.1};
RN [1] {ECO:0000313|RefSeq:XP_014002291.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014002291.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014002291.1; XM_014146816.1.
DR OrthoDB; 2877710at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
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; 8.
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; 13.
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 InterPro; IPR000082; SEA_dom.
DR PANTHER; PTHR44170:SF20; IMMUNOGLOBULIN SUPERFAMILY DCC SUBCLASS MEMBER 3; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF07679; I-set; 6.
DR Pfam; PF13927; Ig_3; 7.
DR Pfam; PF00052; Laminin_B; 3.
DR Pfam; PF00053; Laminin_EGF; 10.
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; 2.
DR SMART; SM00180; EGF_Lam; 8.
DR SMART; SM00409; IG; 13.
DR SMART; SM00408; IGc2; 13.
DR SMART; SM00406; IGv; 4.
DR SMART; SM00281; LamB; 3.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00192; LDLa; 4.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 7.
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; 6.
DR PROSITE; PS50027; EGF_LAM_2; 6.
DR PROSITE; PS50835; IG_LIKE; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51115; LAMININ_IVA; 3.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 4.
DR PROSITE; PS50024; SEA; 1.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00023207};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..3756
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010262777"
FT DOMAIN 88..210
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 408..485
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 555..740
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 774..823
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 824..881
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 955..1132
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1166..1215
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1216..1272
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1544..1731
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1765..1814
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1815..1871
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1871..1966
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1972..2046
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2067..2151
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2158..2269
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2280..2362
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2375..2459
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2466..2554
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2565..2643
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2652..2734
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2738..2821
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2826..2910
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2915..2997
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 3003..3186
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3182..3219
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3222..3260
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3266..3446
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3442..3479
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3481..3514
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3539..3754
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 57..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2209..2236
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 266..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 222..234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 229..247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 241..256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 287..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 294..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 306..321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 327..339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 334..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 346..361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 390..405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 793..802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 852..861
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1185..1194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1244..1253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1256..1270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1784..1793
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1843..1852
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1855..1869
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 3209..3218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3231..3248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3250..3259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3469..3478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3504..3513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3756 AA; 408164 MW; 7B0E7251C20D4E2C CRC64;
MGTRIHSVSG LIVSLIFTCH LINVAQSSKV WGEVPLPEDL DSERTVVQRS QRFLDDDEDF
TADEASGDLP SGEEDGSTPE PTVVTEISTT YYRALVNFTD SIVYRPDMED ISSLSFQEIS
DAVVDTLESE YNRIPGIQTV NVVLIKKMLR QDGVDVFVEL DVGSDYNNND NQIRNVLYGV
VKEGTIASYV TSVQGFQFRR LGEALPPVNP MAVPVVPDLR PCMKDEHTCR DGGCIPLEYL
CDNRPDCNDM SDELDCDKIR PDAVTPTPPT TIPIKKPPRP PGPPGPCKVD QATCQNGECV
PRDYLCDGER DCSDGSDEFR CGTPSPCEPN EFKCKNGRCA LKLWRCDGDN DCEDNSDETD
CPTRGPGDTC APEQFVCLSD RTCIPSSYQC DEEADCPDRS DEYGCTPPTV TSPPEESIQA
VRGETVTFNC VAVGVPTPII TWRLNWGHIP ISGRISMTSE NGGGTLTIRD VKEADQGAYT
CEAINAKGLV FGIPDGVLSL TQKPVLSSSL SSSPGNCPDG HFSVEGRCIS CFCFGITKNC
GSTGRYHSQI NLRFTDEDDF KGVNVTYPSR PGTPPLSSTQ LLINPEDEEF QLVDLSRRFL
ILDSYWTLPR QFLGNKIDSY GGLLKYKVRY TLARGETEPE EKPDVILTGN GQRLVYRRGN
PTPSRVVNKK EIKFTEENWQ HSSGRQVSRE DLMMTLASLE AISIRTVYDN HMVSVALSDI
VMDTTTVEYN IQGNAKEVEE CRCPPGYSGL SCEQCSTGFE RVSGGNFLGS CAGCNCNGHG
SACDPISGHC LSCQHNTEGP QCDKCRPGYF GDPRRGRPDD CKPCPCPYTE TSRRFSDTCF
LDHDSQATCD ACKPGYTGRR CEKCAPGYQG NPLQPNGKCF PNTNSKCDSR GTVNSNSRPC
ACKSNVVGSL CDECKSGAFH LTEENPEGCL QCFCMGVTKQ CASSTWSRDQ VRGGVNGQLF
SLSNSANSRT ITDGITQKGS SEVAYRSFSD IPNDIYYWVL PDSFRGDKVT AYGGELRYTV
RYEPRQRSLV IDGQPDVVLQ GNSIFLEHFS QTKPLPRAPT TVTVTFRESA WRRADGQPCT
REHLLMALAD TTVFMIRATY ADNMAETSLS DIQMDIAVPR STGNEHALEV EECACPQGYK
GPSCQECDVG YTRTGSGLYL GTCERCDCNG HASGCDQETG ACLQCLHNTA GPRCERCLPG
FYGNPVTDGP RACQPCPCPG TSPSNQYSQS CYKDVDGQPT CDNCPPGFTG RRCERCASGY
TGNPQLGQRC SVGNNDLNGN CYNCDQRGSE GCNGNGVCRC KMNVEGPACS NCKQGTFHIS
TDNKDGCLSC FCMGVTQQCS SSSHYRDQVS SVFVPGNFQG FALVNRQHTN RISTGFTVEV
STDGTQLSYS NFDYLGQEPH YWQLPGVYQG DKKEAFFARM RRAHQRDSPW TEEQLRKDTS
IWVLVKSLKG NGTTQAKRAS QEQVKKLDDE IWEIISNFGD KGSPAVSPPF PPSSSSSSSS
SERKIPSHSY HAGSRTPMRP FSPSSSPSGI SSLVLPTRPQ PASPGPSPRL QTKRRGTKNI
VGPPSAHSGP RPAVVSSLYA LVYKRFSLHP DDTLYWQLPD QFKWDKVSSY GGKLKYTINY
VAGQRGTAIE DPDIQIIGND ITLVARQPWQ RGQGTRESRQ FEVVFREENW RRPDGMPATR
EHLMMVLADL DDILVRASYY TEMRSSSISE VSMEVAVPNY SGLAQALEVE QCRCPSAYQG
LSCQDCAPGY TRTGGGLYLG HCELCECNGH SDSCHPETGI CTSCLHNTQG VLCEQCAPGF
FGDPTAGTPE DCQPCACPHT DPDNQFSPTC ESLGNGGYQC TACQPGYTGQ YCERCAPGYV
GNPQDRIKCR PFSTVAASLV VKVYPERVLV AQGSPVTLRC QVTGSPPHYY YWSREDGRLV
TNSADRRGQG EELHIPSVQP SDAGIYVCTC RDQRNTNRSR AEIIVTTVLS KPIEVTIEEP
KAHSVTVGAT VSFICTAKSK SPAYTLVWTR RGNGKLPNRA MDFNGILTIQ NVQPEDAGIY
VCTGSNMFAM DEGTAVLYVP AAEGSEPVAT ATPPVLTIQQ GGRAEFRCTV TGNPTPAIEW
IGGGPGNRMS PNAVVRGGVL TIPAVERGDE GEYVCKALNT HGEHTARAVL YVHSASLPHV
QVSPQRVDIH EGETLRLYCR AGGTPSPGLT WKKQGGQLPP QAIPSHGFHQ FKSNSLDVLQ
KRIDELQTRM ERTDIGTLLI PNIKSSDSGT YLCVGTNSIG SSEARIEVTV NRAIGDTISS
AITIQPSIAD VQEGQSLDLN CFVPGNPPPA VTWRRSSGRL SANHQVLGTQ LRILSASPDD
SGEYICRVVA GPGTPVRQAS VSVSVTATSS RLQTPIISIE PHSAAVRKGE SASFKCRVYS
GAQPVRLEWK LSNNQPLPDN VKIDHYGSVL VITDARPSNQ GTYRCVASNL FGITQSMVSL
IVRESPVATV TPQGPVRVRV GEPINLECQA SGEPRPSVTW HRLDNARKTM LSSPVPMESN
AVMQVLVARP EDSGTYVCAA RNNEGTTETR VEVIVDGGAQ VPTLPRASVP EPLMVVVEGQ
TTTLRCDAHG FPAPKITWSK LRAPLPWRHK VVDNTLVLPS VGRADSGEYI CNATNNMGTT
EVTIMLDVET PPYATSLPDD VAVRVGEVIR LQCLAHGTPP LLFQWTKLNG SLSTRADVQG
GDLQINLAIA EDAGTYKCVA TNKVGTSEAH AKVTVRSPLA VRVSPQVEVK AQGSAVEFTC
SAAGGLGTTM EWLKEGGALP PNHHIKDGVL RIENLDQSNE GVYICRATSV HGQAQDTAKL
TIQALPKVMI NVRTSVQTVM VGNSVEFECQ AIGEPQPTVR WSKVGGLLPA HIVVKGGMLK
IQQVTDADAG QYRCTATNDV GSVQSQVVLN VQSLPQIAAL PELKEVTVGS DAVLPCVASG
YPVPAIKWSK LDGELPPKCI QVVNTLTVPG LTHEDSGTYV CTASNKQGKV EAFTTLKVHD
RVMPHFTQEP LSYLTLPTIK NAYKSFSIKI SFRPDNPDGL ILYAGMIIYN GQKRTMGADF
ISLGLVGGRP EFRFDVGSGM ATIRYPTPIK LGEFHTIELH RNQTQGTIIV DREAPVNGSS
QGKFQGLDLN EELYVGGYPN YTLLAKTASL KTGFIGCIRK LIIQGDEVIF KDLDRSSTGV
SNCPVCTDRP CQNGGTCQDS DASLYKCSCP RGFTGSNCQH HSSLHCHPEA CGPDATCINR
QNSLGYDCRC HLGKSGNKCM DGELVTTPLF DGMDSYIAYP PLTNIHNDLH IEMEFKPMDL
DGLMFFSVGK KMKTEDFVSI EMVDGHVQFR YELGTGQAVL RSPEPVTLGQ WHRLEAGRLD
KDGSLKIDGG REVRRSSPGK AQGLNIHTPM YLGGVPNIDI IPKALNISVL YDGCIGEVSI
NGKKVDLSYS FTDSMAIIQC KDNSPCDRNP CLNGASCMPS AEYEYQCLCK DGFEGERCEV
LKDTCQSSDQ CQNGGSCVNN QCVCPVGFNG PVCGESQVSS FAEALWNLEG SGVNDAPIEY
AVKFYDNGYL SLPKTIFPRS GPDTPETIEL EIKVNTNSKE GLILWQGVES VNGASHFRKM
HASKKVSTSP KHLELGDQGK GKDFISLGLQ NGHLVFSYQL GSGESQIQSR EPINDGRWHK
VTAVRTGKQG YIQIDGGAIR RGQSQGKSIM VNTEGNVYLG GAPDISAMTG GKFSSGLEGC
VRNLSLMNAR PGEQLARPIE LQVPAENGIN VGRCSS
//
