ID A0A3Q7SLN4_VULVU Unreviewed; 2075 AA.
AC A0A3Q7SLN4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
GN Name=AGRN {ECO:0000313|RefSeq:XP_025862859.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025862859.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025862859.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025862859.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025862859.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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_025862859.1; XM_026007074.1.
DR KEGG; vvp:112926137; -.
DR OrthoDB; 2878505at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
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: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; 5.
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; 2.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF07648; Kazal_2; 8.
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; 7.
DR SMART; SM00179; EGF_CA; 4.
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 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:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2075
FT /note="Agrin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018584637"
FT DOMAIN 32..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 909..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 1890..2072
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 983..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 1992..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1031
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1998..2013
FT /note="Polar 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 2075 AA; 219816 MW; C42B3268BC74D8F3 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 CPSRQAPVCG
DDGVTYDNDC VMGRTGAARG LLLQKVRSGQ CQPQDQCPDV CRFNAVCLSR RGRPRCSCDR
VICDGAYRPV CAHDGHTYDN DCWRQQAECR QQRTIPAKHQ GPCDQPLSPC LGVRCPFGAT
CAVKNGEAEC VCQQVCSGIY DPVCGSDGVT YGSTCELEAT ACALGREIRV ARRGPCDRCG
QCRFGALCEA ETGRCVCPSE CVASAQPVCG SDGRTYASEC 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
ETCAEMRCEF GASCVEEAGS ARCVCPTSTC LGANATKVCG SDGVTYGNEC QLRTIACRQG
LDISIQSLGP CQDSVLLAEA VAPGARPTSV PRATSGLSTS KALPPAPSTL PLAPSSTPHS
RPTPRPSPGP 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 AVCEKALHLL
VPAFNGRSFL AFPTLRAYHT LRLTLEFRAL EPQGLLLYNG NAQGKDFLAL TLLGGRVQLR
FDTGSGPAVL TSSVPIEPGR WHHLELSRHW RRGTLSVDGE PLVLGHSPSG TDGLNLDTDL
FVGGIPEDQA SVVLERTSIS VGLKGCIRLL DVNNQRLELS SWPGAAARSS GVGKCGDHPC
LPNPCLNGAP CQALEAGMFH CQCPPGRFGP TCSGDKNPCE PNPCHGAAPC RVLPDGEAKC
ECPRGRGGAI CQTVSERDSS QPFLADFHGF SYLELKGLHT FERDLGEKLA LEVVFLARGP
SGLLLYNGQK TDGKGDFVSL ALHDRFLEFR YDLGKGAAVI RSKEPVALDT WTRVSLERNG
RKGAMRVSDG PRVLGESPKS RKVPHTVLNL KEPLYVGGAP DFSKLARAAA VFSGFDGAIQ
LVSLKGHQLL TQEHVVRSVD VSSFAHHPCT QASGHPCLNG ASCLPREASY ECLCPGGFSG
LHCEKGLIEK SAGDVDALAF DGQTYVEYLN AVTESELTNE IPAPDAPDSG ALPSEKALQS
NHFELSLRTE ATQGLVLWSG KATERADYVA LAIVDGRLQL TYDLGSQPVV LRSTVPVNTN
RWLRVRAHRE QREGSLQVGN EAPVTGSSPL GATQLDTDGT LWLGGLEKLP MGQALPKAYG
TGFVGCLRDV VVGQHPLHLL EDAVTKPELR PCAAP
//
