ID T1PMW7_MUSDO Unreviewed; 2370 AA.
AC T1PMW7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Laminin G domain protein {ECO:0000313|EMBL:AFP64755.1};
DE Flags: Fragment;
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EMBL:AFP64755.1};
RN [1] {ECO:0000313|EMBL:AFP64755.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ALHF {ECO:0000313|EMBL:AFP64755.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:AFP64755.1};
RA Liu N., Zhang L., Li M., Reid W.;
RT "Transcriptome of adult Musca domestica launches a platform for comparative
RT house fly gene expression and characterization of differential gene
RT expression among resistant and susceptible house flies.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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; KA650126; AFP64755.1; -; mRNA.
DR VEuPathDB; VectorBase:MDOA011716; -.
DR VEuPathDB; VectorBase:MDOA014044; -.
DR VEuPathDB; VectorBase:MDOA016122; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 11.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 2.10.25.10; Laminin; 12.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF235; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00008; EGF; 8.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00179; EGF_CA; 11.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 10.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS00022; EGF_1; 13.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 13.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 2: Evidence at transcript level;
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 321..357
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 359..395
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 397..433
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 435..475
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 477..513
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 515..551
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 553..590
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1241..1277
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1282..1489
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1532..1569
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1593..1789
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1785..1821
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1823..1861
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1932..2119
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2115..2152
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2153..2186
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2192..2370
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 93..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2321..2349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2321..2340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 325..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 347..356
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 385..394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 423..432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 465..474
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 503..512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 541..550
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 580..589
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1267..1276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1559..1568
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1811..1820
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1851..1860
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2142..2151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2176..2185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 2370
FT /evidence="ECO:0000313|EMBL:AFP64755.1"
SQ SEQUENCE 2370 AA; 257804 MW; 6AEE4463EED3E2F8 CRC64;
MKTNSENKRN FTSIKVTITK PELTKFQNPH DFQGNNQTCN DLPELRQQQG LIGETSTPFK
FNKNMVKIKH KKIFFFSNKQ QMENWETKEA LNKTHDEGRD DETISATASA VSRTQPTTST
VNVITTPATT VTMSSSTSPL SEILTAMPAV RPTKASEEEY QPLPHLNYQQ QRQHHLHKSN
NNNKEMKNCN QDNELHSTKN SNSPITNTTS SSSAINKSSK RQQVTTSAMN IFRENRNNKN
SHVNELHLGA FYNTLATFIF KQTKMQCGTK SRASSTAPAT PGTRKTRTST STTSTSTTTI
QFVSQLLVLL TMASLVGYAH AGFACLSNPC VFGVCIDGLN SSYSCYCIDG YTGIQCQTNW
DECWSGPCQN GGTCVDGVAY YNCTCPDGFS GANCEENVDE CMSNPCQNGG HCRDRNNGYT
CTCQPGYLGD HCEVDVAVCE TGTGARCQNG GECLEGPGLE FYCECPAGWH GRICQDEINE
CDSSPCQNGG MCVDKLASYV CACPMGYTGT NCEEEILICA DNPCQNNALC LMEEGVPTCY
CVPDYHGEKC EYQYDECQLG PRCMNGGVCI DGVDTFSCSC PPLLTGMLCE CLMIGEDSLD
CNYTARSTTA PPTMKPRPTP ELTTVKSTLE DTTMSGHHGA GGGAAGGGVE DVSESISKSH
EEETEEEEDE DEEGHDKTKG AGDDEDSLEK PSTRPIGGSG FGTGADDDVT PTTAGTHVLH
GSTSASDEED EDGHPSSVGT TDIPTSHDRD RSSSELPGHG GVTEDIEHSG EVTATTATRY
DETSGGSDEA SSTAKPITTG RDTDVYTTVP LSGESGGGSE GATSDSDEDQ TGIYVHPTRP
IYTQHHFTTV ETSIGIEYST SQYSYGMPTY YPTLEIPHVT SKPESDSHIR PYSERPETKS
SEEDEGGHES DGGGDRLPTT PRFVIRPEIA TTAAPFFTEY PEVVVTTKYM DLSPSGGHAP
TTQSPIRGPS YTVTTISSSF DYETIEVSTM SPGISVTVHL PENRTYHPYT PLTTTPSTSI
YHPATTYVSK SDYETTPHYQ GPPTSHPLPH HPDAPMTTGH PLYTEDHHYH GTTTMTPPSL
ASSGTTSATH TSQQVPDVPM TTQASPTTNI LGQGGVVTTQ GPRVATTTEY KPIITYVPPT
TYSVPTYRPA TSAPPTSPPT TMPPTLTTGP PPSAYPTTSP SSHGPSETSP TSAAPAYGTQ
IPVVSSKYPV TEASSEEEES ANTVGTGLGV PASGGSTDIE PHTDCIKMGC YNGGTCVTTS
EGSRCVCRFD RQGALCETPI IIKNAAFSGD SYVSHRIHKD IQHHDSLDTV LPMHVQLKVR
TRATNGLIML AAAQGTKGGH YMALFLQKGL LQFQFSCGLQ TMLLSELETP VNTGHEITIR
AELDFSRNYT HCNASLLVND TLAMSGDQPT WLKLLPPRMH TPETILNTWL HLGGAPQAPI
GLIIELPPSQ SGTGFTGCLH SLKINEDSRE IFGDALDGFG ITECGSLACL SSPCRNGAAC
IKIETNEVDD NGDKVEKWKC KCPSGYMGPT CEISVCEDNP CQYGGTCVQF PGSGYLCLCP
LGKHGHYCEH TYLPPLSIFL DANANFSDLE VALPSFSGSV NGLSSFVAYT VPIPLEYSME
LSFKILPQTM SQIALLAFLG QPGYHDEKSD HLAISFIQGY IMLTWNLGAG PRRIFTQKPI
DFRLDAPRVP YEIKVGRIGR QAWLSVDGKF NITGRSPGSV SRMDVLPILY LGGHEIANFN
TLPHDLPLHS GFQGCIYDVH LKAGQVTVPL QETRGVRGRG VGQCGTRECH RHACQHDGAC
LQHGATFTCI CQEGWYGPLC AQPTNPCDSF NNKCSEESTC VPLVNGYECD CPVGQTGKNC
EEEIHSLSDV SLTGRRSYLA VRWPYLYDNS DKMGAKRSQI ISYRNFTKKL MPPKPIASSN
QHFVMKLLNE VEKQRNFSPV PLMGSKSFEE HHRVQFFFIE FQLRPLSERG LLLYFGSLNK
NMDKKIGFVS LSLQGGVVEF RISGPSNHVT VVRSVRMLAI GEWHKIKMAQ RGRWLTLWVE
GSASSALAPS AEVLVEPDAL LYVGGLKDLS KLPHNAISGF PVPFRGCVRG LVVSGTRIVL
NETNIIESRN IRDCDGTACG GDSCEAGGHC WLDEKLQPHC ICPEYAKGDR CEYSETCKLI
PCKNNGRCLR SGRCSCPNGW GGFYCEIALS KPTTPSFRGN SYLILPPPRI PMKDKRKGPS
MFVRPREAIQ ISLNFSTIEP DGLLLWSEHD RQKFLGLGLE NGHLKIASNL LGSDNDTVST
PSSGFITDGS WHMARIVVDR SHLELQLDGE VIFTEKLASQ ELMQQQQQPS STTSPHRTRS
RNSLLARRGK EPTITYEDLF YLGGFPNLES
//
