ID A0A452IZZ2_9SAUR Unreviewed; 1911 AA.
AC A0A452IZZ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Agrin {ECO:0000256|ARBA:ARBA00016077};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000033666.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000033666.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR Ensembl; ENSGAGT00000038132.1; ENSGAGP00000033666.1; ENSGAGG00000023843.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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:InterPro.
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; 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; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR001190; SRCR.
DR PANTHER; PTHR15036:SF83; AGRIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 4.
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; 6.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00057; FIMAC; 2.
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 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; PS50024; SEA; 1.
DR PROSITE; PS50287; SRCR_2; 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:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..112
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 54..102
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 122..177
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 195..249
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 273..321
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 348..395
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 413..460
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 478..525
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 562..610
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 650..703
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 704..750
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 779..828
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 974..1096
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 1174..1210
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1215..1391
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1392..1429
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1431..1468
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1478..1673
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1656..1694
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1727..1908
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 650..662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 652..669
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 671..680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 704..716
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 706..723
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 725..734
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1200..1209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1419..1428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1458..1467
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1684..1693
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1911 AA; 206053 MW; 1974BD6F1F29A4BB CRC64;
MCGSEVSLRG GERKDKSRHQ HLTPFPHSLC RGMLCGFGAI CERSTTNSSQ ASCVCKKTTC
PVVVAPVCGS DYSTYSNECE LEKAQCNQQR RIKVISKGAC GSKDPCAEVT CSFGSTCARS
TDGQSAKCIC PASCGSAAES TVCGSDGKDY RSECLLNKHA CDKQENVFKK LDGPCDPCRS
TLNDMNRVCR VNPRTRRADL LSRPENCPPK RDPVCGDDGV TYDNECVMGR SGAIRGLEIQ
KVRSGHCQPQ DKCQAECKFN AVCLNRRGTA RCSCDRITCD GAYRPVCARN SRTYSNDCER
QKAECQQKAA IPVKHEGPCD LGIPSPCLSV ECTFGATCVV KNREAVCECQ QVCLSRYDPV
CGSDNRTYGN PCELDAMACV LRKEIKVKHK GPCDRCSKCQ FGAICEAETG RCVCPTECIS
SSQPVCGTDG NTYGSECELH VRACTQQTNI QVAAQGDCKS CGSTVCTFGS KCVGRQCVCP
RCERQPFSQV CGSDGVTYDS PCELQVASCQ QKKAIEVSRT GPCEEECGSG GSGSGEDNEC
EQDRCRQYGG SWDEDVEDDR CVCDFTCLAV PRNPVCGSDG VTYANECELK KTRCEKRQDL
YITSQGACRV IGTLPPPLLV LHCSQTIYGC CPDNTTVALG VGSAGCPSTC QCYPYGSYGG
ACDPTTGQCS CKPGVGGLKC DRCEPGFWNF RGIVTDSKSG CTPCHCDPVG SVRDDCEQMT
GLCSCKTGIT GMKCNQCPNG SKLGMTGCEK DPSAPKSCRE LSCEFGASCV EVSGFAHCEC
PSPLCVEANM TKVCGSDGVT YGDQCQLKTI ACRQGQVIKV KHVGQCHGEL TTRAPDPTET
ATSSLLFEAR PIPRSQPATV RVTTARPATT TWTTQGIRRT TIRPLSTAPV VLATPPPVYS
ESGSAEGSGD PELGSSGDQE ASGAGSAGKC PLLLFSSLTS TPAIERATCY NSPLGCCSDG
KTAAVDAEGS NCPATKVFQG VLILEEVEGQ ELFYTPEMAD PKSELFGETA RSIESALDEL
FRNSDVKKDF KSIRVRDLGQ SSAVRVIVES HFDPATSYTA ADVQRALLKQ IRASKKRPIL
VKKPQEDHIK FMDFDWIPRL FTTTTTTTTA TTMAPITTWR FTTPTAAHIL PPEAMERPST
KMTGPATTRR PTTSTVPATT WRKPTRQPPA TKKPARPCDF HPCLHGGTCE DDGKEFTCSC
PAGKGGAVCE KSIRYFIPGF GGKSYLAFKM MKAYHTVRIA MEFRASELSG LLLYNGQNRG
KDFISLALVN SFVELRFNTG SGTGVITSKV PLEPGKWHQL VVNRNRRNGM LSVDGEPHVN
GESPSGTDGL NLDTDLFIGG VPEDQMTVVA DRTSATAGLK GCIRLLDVNN QMYDLREKGS
DVLYGSGVGE CGNNPCHPNP CHHGAVCHVK EAEMFHCQCL NGYTGPTCAD ERNPCDPSPC
HVSATCLVLP EGGAKCECPM GREGEFCEAV TEQDQTRPFL PEFNSFSYLE LSGLQTFGHE
LQDKMSMEVV FLARNPSGMI FYNGQKTDGK GDFISLALHN GYLEYRYDLG KGAAVLKSKE
PVPLNTWVSV SLERNGRKGV MRINNGERVM GESPVSWQVP HTSLNLKEPL YVGGAPDFSK
LARAAAISTG FDGAVQRVRL LVVENIRSAI EISAFRSHPC SQKPNPCQNG GMCNPRLESY
ECACQRGFSG ARCEKGEKAA GDSEAIAFDG RTYMEYHNAV TKSGGLPVAS VAPFLTQACL
PSPHPAPWCS EKALQENHFE LSIKTDATQG LILWSGKGLE RSDYIALAVV DGYVQMTYDL
GSKPVVLRST VPVNTNQWIQ IKAYRVHRDG SLQVGNEAPI TGSSPLGATQ LDTDGALWLG
GIEKLSVAHK LPKAYSTGFI GCIRDVIVDR QELHLVEDAL NNQTILHCSA K
//
