ID A0A3Q1C030_AMPOC Unreviewed; 2103 AA.
AC A0A3Q1C030;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000018619.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000018619.1}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 80972.ENSAOCP00000018619; -.
DR Ensembl; ENSAOCT00000033214.1; ENSAOCP00000018619.1; ENSAOCG00000023796.1.
DR GeneTree; ENSGT00940000158337; -.
DR Proteomes; UP000257160; Unplaced.
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:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IEA:InterPro.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00104; KAZAL_FS; 9.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.200; -; 3.
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; PTHR15036:SF83; AGRIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 3.
DR Pfam; PF07648; Kazal_2; 9.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF00054; Laminin_G_1; 3.
DR Pfam; PF03146; NtA; 1.
DR Pfam; PF01390; SEA; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 6.
DR SMART; SM00274; FOLN; 6.
DR SMART; SM00280; KAZAL; 9.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
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; 3.
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:UP000257160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..2103
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018537422"
FT DOMAIN 30..164
FT /note="NtA"
FT /evidence="ECO:0000259|PROSITE:PS51121"
FT DOMAIN 200..248
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 268..323
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 350..395
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 412..467
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 487..541
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 547..607
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 625..672
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 708..756
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 798..851
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 852..898
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 927..976
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1165..1287
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1382..1418
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1423..1599
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1600..1637
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1639..1676
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1684..1867
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1863..1899
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1923..2099
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1046..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 31..103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00443"
FT DISULFID 798..810
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 800..817
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 819..828
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 852..864
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 854..871
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 873..882
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1408..1417
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1627..1636
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1666..1675
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1889..1898
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2103 AA; 226993 MW; A77912BF7731359B CRC64;
MGFQRTLRAG RTALLLAGLL VALGQLCAAS CPEKNLEDRE EEANIVLTGT VDEIINMDPV
HNTYSCKVRV WRYLKGKSNV NREILLDGGN RVMIGGFGNP GICDNQVATG DTRIFFLNPA
SESMGPEHKN ELMLNSSLMR ITLRNLEDVE HCVEAHKYII ADKPPHFTPA QPPDGCRGML
CGFGAVCERD PSDPAKAECV CKRVECPSLV APVCGSDSST YTNECELEKA QCNTQRRIKV
LRKGPCSLKD PCTEVTCSYG STCVQSSDGL SAKCMCPLGC EGKSVQTVCG SDGKDYRNEC
ELHQHACKNQ KNIRVQYQGH CDPCKDSENS LSIMCWVEAL TRQPLMFGPP ESCPPNNEPL
CASDGQTYPS ECVMTATGLQ KGIKLKKIHG GQCRQLEECK EECLFNAVCL VEQLNARCSC
DPIECEGTYK PECGKDGHTY TNECLRRKAE CLSKILIPIK HQGPCDLNLP SPCLDKECEH
GAVCVVKNNE PVCECPEACP QTSDPVCGSD GHSYGSPCEM RAMGCALQKA IHIQHKGPCD
EACANCSFGA ICDAQSGLCV CPSECVESHQ PVCGNDGTTY NSECELHVRA CTEQMELRVV
SQGECKTCGS TVCAWGARCV QNKCECPQCS GKAYSPVCGS DGTTYDNECE LRMSSCMQKR
RIDVAKPGSC DEDCGSGGSG SGAESCEQDR CRMFGGSWDE DAEDDRCVCD FACKSVSHNQ
ICGSDGKNYS NECELKKARC EKQQHLLIQN QGPCTADSAV SVPELTPPQH CSLAVYGCCS
DNVTAALGVG QAGCPSTCQC NVYGSYKGTC DPATGQCSCK PGVGGQKCDR CEPGFWNFRG
IVTENMSGCT PCNCDATGSV RDDCEQMSGL CSCKTGVKGM KCNVCPDGSK MGMNGCDKGP
DAPTSCDELE CNFGASCIEV NGQAHCECPS PDCDLKNKTK VCGSDGVTYA DQCQLRTIAC
RQDKDITVQH FGQCTETISE PAERPTPNPP ATIPSSTVAA TITTAVPFHT KMVWGIPPPR
TAPTETVDQP LTTTPFSTLI HNQVNSRHSI HTQPQAPQPT VAATTTTPSP RSSPVPSTAA
SSFEGSGSGE PSGDDQAEEE EEQEEETGSG VPPEASGAEE PVGPVLASST EPTAAVRSSC
DNTEFGCCPD GKTPSSTPEG TNCPSTMKFS GFLHLDQVEG QEIFYTPEME DPKSELFGET
ARSIESALNE LFRKSEVHKD FMSVRVRNLA PSNSILAFVE AHFKPDTSYT VDDIVGALLK
QLKASKDTSI SVKKPEDENI RFTNYGLSTI PIFTTTTMTT TESVTTAALS TTTTTRPPPT
SPYITRRPPG TTRRPSSSRR TTTTSAPVTT PRPTTATATA TTTVPPPATT ITHVRGRTHH
KPQKPCDSHP CLHGGTCEDD GNDFSCKCPS GRGGSVCEKV IKYFIPSFGG QSYLAFQTMS
AYHTVRIAME FRASEMTGLL LYNGQDGKKD FISLALVSGR MELRFNTGSG TGTLVSKVQV
SQGRWHQLVV TRNRRNAMLS VDNEPHIEGE SPRGTDGLNL DTHLFIGGVP EEMKQDVRER
TAVATGLVGC IRLLDVNNRV LNLQETGGDS LYGSGVGECG NNPCQPNPCK NAAACQVKEA
EMFHCKCSKG FWGPTCADVH DPCEPNRCHP SSQCQALPEG GYKCECPMGR EGRHCEKVAE
RRGSYMPLFN GDSYLELKGL HLYGHDLRQK VSMTVVLMAN DSNGVIFYNG QKSDGKGDFI
SLSLNDGILE FRYDLGKGSA IIRSKEAIQL NVWNTINLER SNRKGEIMVN KKDPVRGEAP
NMHVDLNLKE SLFVGGAPDY SRLARVAALT EGFKGTIQKI ILMGTPILRE ENALRSSNVA
MFQDHPCSQE PCHNGGRCNP QLDTYECVCL NGFSGGHCQN TIYEKSAGET EAVAFDGRTF
IEYHNAVTKS PESLENPSDQ SEKALLVNKF ELSIRTEATQ GLVLWSGKGI ERSDYIALAI
VDGHVQMTYD LGSKPVVLRS SVRVDTNRWI RIKASRALRD GSLQVGNEAA VTGSSPLAAT
QLDTDGALWL GGLEELAVAR RLPKAYSTGF VGCIKDVVVD GVDLHLVEDA LNSPKILHCS
AAK
//
