ID A0A494C1I6_HUMAN Unreviewed; 1963 AA.
AC A0A494C1I6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
GN Name=AGRN {ECO:0000313|Ensembl:ENSP00000499046.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000499046.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000499046.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H.,
RA Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C.,
RA Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R.,
RA Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.,
RA Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.,
RA Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R.,
RA Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D.,
RA Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A.,
RA Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S.,
RA Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A.,
RA Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S.,
RA Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A.,
RA Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L.,
RA Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z.,
RA Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C.,
RA Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M.,
RA Langford C.F., Pandian R.D., Porter K.M., Prigmore E.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2] {ECO:0000313|Ensembl:ENSP00000499046.1}
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 EMBL; AL645608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; A0A494C1I6; -.
DR MassIVE; A0A494C1I6; -.
DR PeptideAtlas; A0A494C1I6; -.
DR Antibodypedia; 12009; 238 antibodies from 27 providers.
DR Ensembl; ENST00000651234.1; ENSP00000499046.1; ENSG00000188157.15.
DR HGNC; HGNC:329; AGRN.
DR VEuPathDB; HostDB:ENSG00000188157; -.
DR GeneTree; ENSGT00940000158337; -.
DR ChiTaRS; AGRN; human.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000188157; Expressed in right uterine tube and 188 other cell types or tissues.
DR ExpressionAtlas; A0A494C1I6; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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; 2.60.120.200; -; 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; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
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; 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; 4.
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; 3.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 9.
DR SUPFAM; SSF82671; SEA domain; 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; PS50024; SEA; 1.
PE 1: Evidence at protein level;
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00023207};
KW Proteomics identification {ECO:0007829|EPD:A0A494C1I6,
KW ECO:0007829|MaxQB:A0A494C1I6};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..139
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 159..214
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 240..286
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 303..358
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 384..431
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 436..496
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 503..561
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 599..647
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 688..741
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 742..788
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 817..866
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1025..1147
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1224..1262
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1267..1443
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1444..1481
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1483..1520
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1530..1717
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1713..1752
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1778..1960
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 890..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 688..700
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 690..707
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 709..718
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 742..754
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 744..761
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 763..772
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1233..1250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1252..1261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1471..1480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1510..1519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1742..1751
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1963 AA; 205568 MW; 30A2BC4BDD0793DC CRC64;
MPPLPLARDT RQPPGASLLV RGFMVPCNAC LILLATATLG FAVLLFLNNY KPGTHFTPVP
PTPPDACRGM LCGFGAVCEP NAEGPGRASC VCKKSPCPSV VAPVCGSDAS TYSNECELQR
AQCSQQRRIR LLSRGPCGSR DPCSNVTCSF GSTCARSADG LTASCLCPAT CRGAPEGTVC
GSDGADYPGE CQLLRRACAR QENVFKKFDG PCDPCQGALP DPSRSCRVNP RTRRPEMLLR
PESCPARQAP VCGDDGVTYE NDCVMGRSGA ARGLLLQKVR SGQCQGRDQC PEPCRFNAVC
LSRRGRPRCS CDRVTCDGAY RPVCAQDGRT YDSDCWRQQA ECRQQRAIPS KHQGPCDQAP
SPCLGVQCAF GATCAVKNGQ AACECLQACS SLYDPVCGSD GVTYGSACEL EATACTLGRE
IQVARKGPCD RCGQCRFGAL CEAETGRCVC PSECVALAQP VCGSDGHTYP SECMLHVHAC
THQISLHVAS AGPCETCGDA VCAFGAVCSA GQCVCPRCEH PPPGPVCGSD GVTYGSACEL
REAACLQQTQ IEEARAGPCE QAECGSGGSG SGEDGDCEQE LCRQRGGIWD EDSEDGPCVC
DFSCQSVPGS PVCGSDGVTY STECELKKAR CESQRGLYVA AQGACRGPTF APLPPVAPLH
CAQTPYGCCQ DNITAARGVG LAGCPSACQC NPHGSYGGTC DPATGQCSCR PGVGGLRCDR
CEPGFWNFRG IVTDGRSGCT PCSCDPQGAV RDDCEQMTGL CSCKPGVAGP KCGQCPDGRA
LGPAGCEADA SAPATCAEMR CEFGARCVEE SGSAHCVCPM LTCPEANATK VCGSDGVTYG
NECQLKTIAC RQGLQISIQS LGPCQEAVAP STHPTSASVT VTTPGLLLSQ ALPAPPGALP
LAPSSTAHSQ TTPPPSSRPR TTASVPRTTV WPVLTVPPTA PSPAPSLVAS AFGESGSTDG
SSDEELSGDQ EASGGGSGGL EPLEGSSVAT PGPPVERASC YNSALGCCSD GKTPSLDAEG
SNCPATKVFQ GVLELEGVEG QELFYTPEMA DPKSELFGET ARSIESTLDD LFRNSDVKKD
FRSVRLRDLG PGKSVRAIVD VHFDPTTAFR APDVARALLR QIQVSRRRSL GVRRPLQEHV
RFMDFDWFPA FITGATSGAI AAGATARATT ASRLPSSAVT PRAPHPSHTS QPVAKTTAAP
TTRRPPTTAP SRVPGRRPPA PQQPPKPCDS QPCFHGGTCQ DWALGGGFTC SCPAGRGGAV
CEKVLGAPVP AFEGRSFLAF PTLRAYHTLR LALEFRALEP QGLLLYNGNA RGKDFLALAL
LDGRVQLRFD TGSGPAVLTS AVPVEPGQWH RLELSRHWRR GTLSVDGETP VLGESPSGTD
GLNLDTDLFV GGVPEDQAAV ALERTFVGAG LRGCIRLLDV NNQRLELGIG PGAATRGSGV
GECGDHPCLP NPCHGGAPCQ NLEAGRFHCQ CPPGRVGPTC ADEKSPCQPN PCHGAAPCRV
LPEGGAQCEC PLGREGTFCQ TASGQDGSGP FLADFNGFSH LELRGLHTFA RDLGEKMALE
VVFLARGPSG LLLYNGQKTD GKGDFVSLAL RDRRLEFRYD LGKGAAVIRS REPVTLGAWT
RVSLERNGRK GALRVGDGPR VLGESPKSRK VPHTVLNLKE PLYVGGAPDF SKLARAAAVS
SGFDGAIQLV SLGGRQLLTP EHVLRQVDVT SFAGHPCTRA SGHPCLNGAS CVPREAAYVC
LCPGGFSGPH CEKGLVEKSA GDVDTLAFDG RTFVEYLNAV TESELANEIP VPETLDSGAL
HSEKALQSNH FELSLRTEAT QGLVLWSGKA TERADYVALA IVDGHLQLSY NLGSQPVVLR
STVPVNTNRW LRVVAHREQR EGSLQVGNEA PVTGSSPLGA TQLDTDGALW LGGLPELPVG
PALPKAYGTG FVGCLRDVVV GRHPLHLLED AVTKPELRPC PTP
//
