ID A0A8I3P8Z0_CANLF Unreviewed; 2064 AA.
AC A0A8I3P8Z0;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
GN Name=AGRN {ECO:0000313|Ensembl:ENSCAFP00845029993.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00845029993.1, ECO:0000313|Proteomes:UP000805418};
RN [1] {ECO:0000313|Ensembl:ENSCAFP00845029993.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Labrador retriever {ECO:0000313|Ensembl:ENSCAFP00845029993.1};
RA Eory L., Zhang W., Schoenebeck J.;
RT "Long-read based genome assembly of a Labrador retriever dog.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCAFP00845029993.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845029993.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCAFP00845029993.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845029993.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: This released fragment is important for agrin signaling and
CC to exert a maximal dendritic filopodia-inducing effect. All 'z' splice
CC variants (z+) of this fragment also show an increase in the number of
CC filopodia. {ECO:0000256|ARBA:ARBA00054843}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000256|ARBA:ARBA00004498}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
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_005620419.2; XM_005620362.4.
DR RefSeq; XP_038522194.1; XM_038666266.1.
DR Ensembl; ENSCAFT00845038300.1; ENSCAFP00845029993.1; ENSCAFG00845020649.1.
DR GeneID; 479574; -.
DR CTD; 375790; -.
DR GeneTree; ENSGT00940000158337; -.
DR OrthoDB; 5983569at2759; -.
DR Proteomes; UP000805418; Chromosome 5.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-ARBA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043236; F:laminin binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProtKB-ARBA.
DR GO; GO:0061024; P:membrane organization; IEA:UniProtKB-ARBA.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-ARBA.
DR GO; GO:0043113; P:receptor clustering; IEA:InterPro.
DR GO; GO:0050808; P:synapse organization; IEA:UniProtKB-ARBA.
DR GO; GO:0099536; P:synaptic signaling; IEA:UniProtKB-ARBA.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00104; KAZAL_FS; 9.
DR CDD; cd00110; LamG; 3.
DR FunFam; 3.30.60.30:FF:000013; Agrin; 1.
DR FunFam; 3.30.60.30:FF:000016; Agrin; 1.
DR FunFam; 3.30.60.30:FF:000032; Agrin; 1.
DR FunFam; 2.10.25.10:FF:000228; agrin isoform X1; 1.
DR FunFam; 2.40.50.120:FF:000008; agrin isoform X1; 1.
DR FunFam; 2.10.25.10:FF:000492; agrin isoform X5; 1.
DR FunFam; 2.10.25.10:FF:000095; Notch, isoform B; 1.
DR FunFam; 2.60.120.200:FF:000031; NtA agrin; 1.
DR FunFam; 3.30.60.30:FF:000019; NtA agrin; 1.
DR FunFam; 3.30.70.960:FF:000001; NtA agrin; 1.
DR FunFam; 2.10.25.10:FF:000134; Transmembrane agrin; 1.
DR FunFam; 2.10.25.10:FF:000140; Transmembrane agrin; 1.
DR FunFam; 2.60.120.200:FF:000027; Transmembrane agrin; 1.
DR FunFam; 2.60.120.200:FF:000045; Transmembrane agrin; 1.
DR FunFam; 3.30.60.30:FF:000008; Transmembrane agrin; 1.
DR FunFam; 3.30.60.30:FF:000015; Transmembrane agrin; 1.
DR FunFam; 3.30.60.30:FF:000018; Transmembrane agrin; 1.
DR FunFam; 3.30.60.30:FF:000022; Transmembrane agrin; 1.
DR FunFam; 3.30.60.30:FF:000024; Transmembrane agrin; 1.
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; 5.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_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; IPR050372; Neurexin-related_CASP.
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; 2.
DR Pfam; PF00053; EGF_laminin; 2.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF07648; Kazal_2; 8.
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; 7.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 3.
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; 3.
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; 1.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000805418};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2064
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044006161"
FT DOMAIN 33..159
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 347..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 491..538
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 543..603
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 621..668
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 795..848
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 849..895
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 924..973
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1136..1258
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1336..1374
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1379..1555
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1556..1593
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1595..1632
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1642..1829
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1825..1864
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1875..2061
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 985..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1982..2001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1020
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1098
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1322
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00443"
FT DISULFID 795..807
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 797..814
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 816..825
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 849..861
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 851..868
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 870..879
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1345..1362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1364..1373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1583..1592
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1622..1631
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1854..1863
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2064 AA; 218696 MW; 4176E1380CA3D130 CRC64;
MASLRRSGPA PLQLLLLLLV VAARALPSAD GTCPERALER REEEANVVLT GTVEEILNVD
PVQHTYSCKV RVWRYLKGKD MVTQESLLDG GNKVVIGGFG DPLICDNQVS TGDTRIFFVN
PAPPYLWPAH KNELMLNSSL MRITLRNLEE VEHCVEDKPG THFTPAPPTP PDACRGMLCG
FGAVCEPSAG GSGRASCVCK KSACPAVVAP VCGSDASTYS NECELQRAQC SQQRRIRLLS
RGPCGSRDPC SNVTCSFGST CVRSADGQTA TCLCPATCRG PPEGPVCGSD GADYPSECQL
LRLACTRQEN IVKKFDGPCD PCQGTHHDLS RVCRVHPRTR HPEMLLRPES CPSQPAPVCG
DDGVTYDNDC IMGRTGATRG LVLQKVRSGQ CQPQDQCPDV CRFNAVCLSR RGRPRCSCDR
VICDGAYRPV CAHDGHTYDN DCWRQQAECR QQRTIPAKHQ GPCDQPLSPC LGVRCPFGAT
CAVKNGEAEC VCQQVCSGIY DPVCGSDGVT YGSTCELEAT ACALGREIRV ARRGPCDRCG
QCRFGALCEA ETGRCVCPSE CVASAQPVCG SDGHTYASEC ELHVHACTHQ ISLHVVSAGH
CQTCGDTVCA FGAVCLAGQC VCPRCERPPP GPVCGSDGVT YDSACHLREA ACQQQTQIEE
ARAGPCEQAE CGSGGSGSGE DGECEQELCQ QHGGVWDEDS EDGPCVCDFS CHSVLRSPVC
GSDGLTYGTE CELKKARCES RRELYVTAQG ACRGPTLAPL LPAVPPHCTQ TPYGCCQDNV
TAARGVGLAG CPSSCQCNPH GSYSGTCDPT TGQCSCRPGV GGLKCDRCEP GFWNFRGIVT
DGRSGCTPCS CDPRGAVRDD CEQMTGLCSC KPGVAGPKCG QCPDGHALGP GGCETDSLAP
ETCAEMHCEF GASCVEEAGS ARCVCPTSTC PGASATKVCG SDGVTYGNEC QLRTIACRQG
LDISIQSLGP CQDSVLLAET VAPGARPTSV PRATSGLSTS KALPPAPSTL PLAPSSTPHS
RPTPRPSPGS RTTASIPRTV TRPVLTMPPT APATAANLAT SAFGESGSAD GSGDEGLSGD
LEASGTGSGG LEPPEGGSAV TPEPPMERAS CYNSPLGCCS DGKTPSLDAE GSNCPATKAF
QGVLELEGVE GQELFYTPEM ADPKSELFGE TARSIESTLD DLFRNSEVKK DFRSVRLRDL
GPGSSVRAIV DVHFDPATTF RAPDVGQALL RQIQASRRRS LGVRRPLQEH VRFMDFDWFP
AFFTGATTGA TPAAATARAT TVAHLPPAGT QWALYPSHTS RPVGRTTAPP TTRQPPTTAP
RRVPGRRPLP PGTQQPPKPC DSQPCLHGGT CQDQDSGGGF TCSCPVGRRG AVCEKALYLS
VPAFNGRSFL AFPTLRAYHT LRLALEFRAL EPQGLLLYNG NAQGKDFLAL TLLGGRVQLR
FDTGSGPAVL TSSVPIEPGR WHRLELSRHW RRGTLSVDGE PLVLGHSPSG TDGLNLDTDL
FVGGIPEDQA SVVLERTSIS VGLKGCIRLL DVNNQRLELS SWPGAAARSS GVGECGDHPC
LPNPCLDGAP CQALEAGMFH CQCPPGRFGP TCSGDKNPCE PNPCHGAAPC RVLPDGEAKC
ECPRGRGGAI CQTVSERDSS QPFLADFHGF SYLELKGLHT FERDLGEKLA LEVVFLARGP
SGLLLYNGQK TDGKGDFVSL ALHDRFLEFR YDLGKGAAVI RSKEPVALDT WTRVSLERNG
RKGAMRVSDG PRVLGESPKS RKVPHTVLNL KEPLYVGGAP DFSKLARAAA VFSGFDGAIQ
LVSLKGHQLL SQEHVVRSVD VSSFAHHPCT QASGHPCLNG ASCLPREASY ECLCPGGFSG
LHCEKGLIEK SAGDVDALAF DGQTYVEYLN AVTESELTNE IPAEKALQSN HFELSLRTEA
TQGLVLWSGK ATERADYVAL AIVDGRLQLT YDLGSQPVVL RSTVPVNTNR WLRVRAHREQ
REGSLQVGNE APVTGSSPLG ATQLDTDGTL WLGGLEKLPI GQALPKAYGT GFVGCLRDVV
VGQRPLHLLE DAVTKPELRP CAAP
//
