ID A0A1S3MEU6_SALSA Unreviewed; 1921 AA.
AC A0A1S3MEU6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
DE AltName: Full=Activin-binding protein {ECO:0000256|ARBA:ARBA00042260};
GN Name=LOC106572186 {ECO:0000313|RefSeq:XP_014001599.1};
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_014001599.1};
RN [1] {ECO:0000313|RefSeq:XP_014001599.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014001599.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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_014001599.1; XM_014146124.1.
DR GeneID; 106572186; -.
DR CTD; 375790; -.
DR OrthoDB; 2878505at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043236; F:laminin binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0043113; P:receptor clustering; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00104; KAZAL_FS; 9.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 3.30.60.30; -; 9.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR003884; FacI_MAC.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR004850; NtA_dom.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR10913:SF45; AGRIN; 1.
DR PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF07648; Kazal_2; 9.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF03146; NtA; 1.
DR Pfam; PF01390; SEA; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 6.
DR SMART; SM00274; FOLN; 5.
DR SMART; SM00280; KAZAL; 9.
DR SMART; SM00282; LamG; 2.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 9.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 2.
DR PROSITE; PS51465; KAZAL_2; 9.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
DR PROSITE; PS51121; NTA; 1.
DR PROSITE; PS50024; SEA; 1.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
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}; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1921
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010244656"
FT DOMAIN 28..162
FT /note="NtA"
FT /evidence="ECO:0000259|PROSITE:PS51121"
FT DOMAIN 198..246
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 266..321
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 339..393
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 410..465
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 485..539
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 545..605
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 612..670
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 706..754
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 796..849
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 850..896
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 925..974
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1155..1277
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1350..1386
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1391..1567
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1568..1605
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1607..1644
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1652..1839
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1835..1871
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 981..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1753..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 29..101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00443"
FT DISULFID 796..808
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 798..815
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 817..826
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 850..862
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 852..869
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 871..880
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1376..1385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1595..1604
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1634..1643
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1861..1870
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1921 AA; 208500 MW; 7353D39D631E6496 CRC64;
MVSQRRPTHL YGWALTIVAV FCQRCHGSCP EKDLEKREEE ANVVLTGTVE EIMNMDPVHN
TYSCKVRVWR YLKGKTMVNG EVLLDGGNKV MIGGFGDPVI CDNQVATGDT RIFFVNLAPE
YMWPAHKNEL MLNSSLMRIT LRNLEEVEHC VDDHRMINAD KPVHFTPAQP PDGCRGMLCG
FGAVCEREAA DPSKAECVCK KMACPSVVAP VCGSDSSTYS NECELEKAQC NTQRRIKVLR
KGPCALKDPC SEVICSYGST CIQSSDGLSA KCMCPLSCDG KPEQVMCGSD GQDYRNECEL
HKQACHTKKN IRLQRQGSCN PCKGLENNLN VACRVEPRTH QRLNIPRPES CPAVNEPLCA
SDGQMYESEC HMKRTGMQKG IELKQIHPGR CKKQEECREE CKFNGVCQVE RLGMRCSCEP
IQCDGTYKPL CGKDGHTYIN DCERRRAECQ AKAHIPVKQQ GPCDLHTPSP CLGKACEFGA
ACVVKNNEPV CECHGACPQT PDLVCGSDGH SYGSQCEMKA MGCALQKEIH IQHRGPCDEA
CANCSFGAIC DGQSGRCVCP QECVESHQPV CGSDGSTYDS ECELHVRACT EQLDLRVLAQ
GECKTCGSAV CAWGARCVQN KCECPQCQGQ AFSPVCGSDG FTYDNTCELG VASCVLKKKI
EAAKPGSCDE ECGSGGSGSG IESCEQDRCR MFGGSWDEDA EDDRCVCDFD CHRVPRNPVC
GSNGKTYSNE CQMKKARCEK QEHLLIQNQG PCTAISATSP TKLTAQEHCS LSVYGCCRDN
KTAALGVGLA GCPSTCQCNP YGSYKGTCDP GSGQCSCKPG VGGQKCDRCD PSFWNFRGIV
TDNLSGCTPC NCDAVGSVRD DCEQMSGLCS CKTGVKGMKC NVCPDGSKMG MSGCDKGADA
PTSCDELDCK FGALCDEVNG QAHCECPSPD CDEKNKTKVC GSDGVTYADQ CQLRTIACRQ
DKHITVERFG QCTESIIEPA GRPTLYPPTS HAAATTPSTA HVRLKSPHYD TSLSPWDDDQ
TDGSTASFVD ALPPPMVTES ALTTNRPVTT PRHPPHSTTP RLLGHTSPGS SPTAFEDSGS
GEPSGDDQVA EEEENGEDGS AGVLEASGEE PVDPTAAATT IPTAEDRSSC DNTPFGCCPD
SKTASSSPEG ANCPPTMRFS GFLHLDQVEG QEVFYTPEME DPKSELFGET ARSIESALNE
LFRKSEVQKD FMSVRVRSLA PSNSILAFVE AHFDSETRYT VEDIEGALLK QLKAAKETAI
MVKKPEEENI RFTNYGLSSL PYFTTTTTTT ATTPTASPSP FITSRPPGTT RRPYTSRRTT
TAPSPVTTPA PTTTITPLHR TRPVPHHTKA QRPCDSHPCR HGGTCEDDGA DFTCICPAGR
GGAVCEKLIK YFIPSFGGKS YLAFDTMKAY HTVRIAMEFR AAEMTGILLF NGQDGKKDFL
SLTLVNGKVE LKFNTGSGTG TLVSKVQVKQ GRWHQLVVTR NRRNAMLSVD NETHIDGASP
PGTDGLNLDT HLFIGGVPED MMTDVKERTS IGTGLVGCVR MLDVNNLVYN LQEKSGNVLY
GTGVGECGNN PCQPNPCKNG APCQVKEAEM FHCKCINGYS GPTCADTHNP CEPNRCHPSS
QCQVQPEGGY KCECPMGREG RHCEKVSEKK GAYMPFFSGD SYLELKGLHT YGHDLHQKVS
MTVVLMANDS NGMIFYSGQK TDGKGDFISL SLNDGILEFR YDLGKGPAVI RSKDKIKMGV
WNTVNLERAN RKGEININGK DPVRGESPKS RKNQHTALNL KESLFVGGAP DFSRLARAAS
LKDGFKGTIQ KITLMGTPIL RQENALHSSD VAMFEGHPCS REPCHNGGRC NPLLESYECV
CLLGFTGTHC QNTIFEKSAG ETESIAFDGR TFIEYHNAVT KSQLTNEIPD PESLENPSEQ
R
//
