ID A0A3Q3CXN3_HAPBU Unreviewed; 1943 AA.
AC A0A3Q3CXN3;
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 Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000033083.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000033083.1}
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 Ensembl; ENSHBUT00000026582.1; ENSHBUP00000033083.1; ENSHBUG00000019878.1.
DR GeneTree; ENSGT00940000158337; -.
DR OMA; AMEISPF; -.
DR Proteomes; UP000264840; 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: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; 2.
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; 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; 5.
DR SMART; SM00274; FOLN; 5.
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; 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:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1943
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018593446"
FT DOMAIN 30..164
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 346..388
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 404..459
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 486..533
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 539..599
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 617..664
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 702..750
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 789..842
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 843..889
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 918..967
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1009..1131
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1214..1250
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1255..1431
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1432..1469
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1471..1508
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1516..1699
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1695..1731
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1763..1939
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1148..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 31..103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00443"
FT DISULFID 789..801
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 791..808
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 810..819
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 843..855
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 845..862
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 864..873
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1240..1249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1459..1468
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1498..1507
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1721..1730
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1943 AA; 210705 MW; AD75042487710F88 CRC64;
MGSQRTLRAG RTGLLLAGLL VAVWQLCAAN CPEKELEDRE EEANIVLTGT VDEIINKDPV
HNNYSCKVRV WRYLKGKSSV NREILLDGGN KVMIGGFGNP GICDNQVSVG DTRIFFLNPA
PDYMRPEHRN ELMLNSSLMR ITLRNLEAVE HCVEAHKYIV ADNPLHFAPT VDGCRGMLCG
FGAVCERNPN DPSKGECVCK KVDCPSFVAP VCGSDSSTYT NECELEKAQC NAQRRIKVLS
KGACSLKDPC TEVACSYGST CVQSSDGLSA KCMCPLGCEG KPKQVVCGSD GKDYVNECEL
HQHACKNKKN IRVQYQGHCD PCKNVLNCRV EPLTRQPLKF VPLELCPLSD EPLCASDGRT
YPSECAMRAT GIQKGVTLRK IHAGQCTTLD ECKDCPFYGV CLVEQLSARC SCDPIECDGT
YKPLCGKDDN TYTNDCMRRK AECLSKTPIG TKHLGPCDLN IPSPCLHVAC SHGAECVVKN
NEAVCECSEA CPQTSDPVCG SDGQTYGSPC EMRLMGCALQ KEISIQHKGP CDEACANCSF
GAICDAQSKQ CVCPSECVKS HQPVCGSDGT TYNSECELHV RACKQQMDLR VVGQGECKTC
GNTVCAMGAR CVQNRCECPP CSGEPYSPVC GSDGTTYDNE CELRRHSCTQ MTRIDVARLG
SCDEDCGSGG SGSGQESCEQ DRCLVFGGTW YEDAEDESDR CLCEYSCTSV PHSLVCGSDG
KNYSNECELK KARCEKREHL LIQNQGPCAA VSLPDPTVSE HCSVSVYGCC SDNVTAALGV
GQAGCPATCQ CNIYGSYKGT CDPTTGQCSC KPGVGGQKCD RCEPGFWNFR GIVTENMSGC
TPCNCDATGS VRDDCEQMSG LCSCKTGVKG MKCNVCPDGS KMGMNGCDKG PEAPTSCEEL
QCNYGATCIK VNGQAHCECP SPDCDLKNKT KVCGSDGVTY ADQCQLRTIA CRQDKDITVQ
HFGQCTGPTM ASTTLPTLED RSSCDNTEFG CCPDGKTPSS TPEGANCPST MRFSGSLHLD
QVDGQDLIYT PEMEDPKSEL FGETARSIEG ALNELFRKSA VHKDFMSVRV RNLAPSNSIL
AYVEAHFKPD TRFTVEDIVG ALLKQLKASK DTSISVKKPE DENIRFTNYG LSSISIFTTT
TTTTTASVTT AAPTTSTRPP TTSPYITRRP TATTRRPFSG RHKLVPVTSP LTTTALPPAT
TVARFTTRPY HKVLQKPCDS HPCLHGGTCE ENGSEFNCKC PAGRGGTVCE KVIKYYIPSF
GGQSYLAFPT MSAYHTVRIA MEFRASEMDG ILLYNGQDRK KDFISLALVN GRVELRFNTG
SGTGTALSKV QISQGRWHQL VVTRNRRNAM LSVDSEPHIE GESPRGTDGL NLDTNLFIGG
VPEDIEQDVK ERTGLAVGLV GCIRMLDVNN RNLNLQENGG ESLYGSGVGE CGNNPCLPNP
CKNGGACQVK EAEMFHCKCS KGFWGLTCAD VHDPCSPTRC HPSSQCQAQP EGGYKCECPM
GREGRHCENV VERQGAYMPL FNGDSYLELK GLHLYGHDLR QKVSMTVVFM ANDSNGLIFY
NGQKSDGRGD FISLSLSGGF LEFRYDLGKG PATIRSKERI QLNVWNTINL ERSNRKGEIM
VNKKGAVRGE APNQHVDLNL KESLFVGGAP DYSRLARAAA LTEGFKGTVQ QITLMGTPIL
REENALRSSS VAMFQNHPCS REPCHNGGRC KPQLDTYNCE CLSGFSGQHC QNTIHEKSAG
ETEAIAFDGR TFIEYHNAVT RSQLTNEIPD PESLENPSDQ SEKALLVNKF ELSIRTDTTQ
GLVLWSGKGV ERSDYIALAI VDGHVQMTYD LGSKPVVLRS TVRVDTNSWI RIKASRALRD
GSLQVGNEAP VTGSSPLAST QLDTDGALWL GGLEELPVAR RLPKAYSTGF VGCIKDVVVD
GVDLHLVEDA LNSPRILHCS AAK
//
