ID A0A0N4ZPD7_PARTI Unreviewed; 1981 AA.
AC A0A0N4ZPD7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Laminin subunit beta-1 {ECO:0000313|WBParaSite:PTRK_0001039700.1};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001039700.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001039700.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 131310.A0A0N4ZPD7; -.
DR WBParaSite; PTRK_0001039700.1; PTRK_0001039700.1; PTRK_0001039700.
DR Proteomes; UP000038045; Unplaced.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF444; -; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 9.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460}.
FT DOMAIN 222..456
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 653..703
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 704..745
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 743..961
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 967..1014
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1015..1061
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1062..1111
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1173..1224
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1225..1273
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1274..1329
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1330..1376
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1381..1441
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1927..1954
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 675..684
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 687..701
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 967..979
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 969..986
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 988..997
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1015..1027
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1017..1034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1081..1090
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1197..1206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1225..1237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1227..1244
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1246..1255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1302..1311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1330..1342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1332..1349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1351..1360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1981 AA; 225995 MW; 68EB134CB679C221 CRC64;
MFYFSDNNAS EFWTYLLPMF NTIKLERIGQ FFSRYFIEKC EICQPRLFDF SYYKSLKFID
TSLLVHTEYY EEDCRMIKWL IKSLRNTTPV TIIVRILGNN GNNNGMNEGT YKDLLSSSYA
KEVVRNINNS NHYIKLELNT SSWDIETWFE SLIMGKPRNE EILPESFLLS LTVIKYFSFW
CFEEDSFFIP DSCCGVKIEC HCFWSDDMEC SCTKCEEEDL CIGHSCYPAT GNLLIGRKNQ
LSVTSTCGLK QIEKYCIVSN LVGNSSCYQC DSRRPNVNNH RIENVIKEKN ENKYQRWWQA
ENGKENVSIR LDLEAEFHFT HLIMTFKNFR PSAMLIERSS DYGKKWEVYR YFAYDCANSF
PKIREIVPKN HGDVVCTDRY SSISPSNGGE LIYKVVNPQI PTINPYAEEV AKLLRITNLR
INFTKLHTLG DDLLDHRQDI KKKYYYGLYE LIIRGSCSCY GHAQKCIPMD NNINNVRYYN
YQEQVPDMVY GKCLCTHNTK GLNCEFCDDF FNDLPWKPGF GNETNECKRC ECNNHARSCH
FDEGVYINSG NTSGGVCDDC QHNTMGIHCE VCKPYFYKDV NLPFNSPHAC KACSCDIRGS
LYNGICESEN DEERNLISGK CYCKRFVDGN DCSYCKDGFW NLNENNDDGC EECSCNILGT
INNEGCNKET GECICKRFVT GDKCNSCVEN YYGLSEDLDG CKDCDCDIGG SLSSQCDNVT
GQCICKKHFT GRRCDIPEDS FYCPNLDFYT FEGEDSVRSG KESIIEYREK KSKNYFQKWS
GTGYVRVKEG SELNFMIGRV YKTLLYNIII RYDSERNSIG WENVEIILSR PNIINNENNG
SCKGYNVDND YMIIRLEGNK KYKEITPSIC LEEGIDYQLK IIFREKITNY NDRSASILID
SIIITPPLDE LEIFNNMETG RYHLDRYTIN YCRHLILLLT SVNDLPTICQ KYTCSIAGSM
IDKGIQCDCD KTGSVSALCN IYGGECSCKK NVIGRRCDKC DVGTYGFSPN GCLPCECDSV
GALDNICDRE SGQCLCNKNE ITGRQCNECY EGSWNFPNCQ LCSCNGHTEI CDQKNGTCLS
CNENTKGYNC ERCRDGYYGD PRIEVNIPCK PCMCPGGPDS GNYNAKSCSF NYISGGTLAL
CHCKKGYVGN TCDECDINYW GNPKEVGGSC EKCECSGNVD PNVEGNCDKN TGECMKCLYH
TTGINCELCD DGFFGNGAER SCEPCACNKL GSISDVCDKN TGSCSCLPNV VGDKCNSCAE
NHYNLNSGKG CLKCECDPNG VVLDDKGEPI LSCDLSNGQC QCKEGRGGKK CSECKNYFWG
NPSLNDCTEC NCNRIGSSSA QCNKDNGSCE CRTGYGNVTC DSCAYGYKGQ FPYCESCGEC
FTNWDEILKN LNNEVDXLIR KGKNIEDKGV PSFYDKQFNI MESKLDDIKK MLNKNKITEE
ELYKLSHGAI LFDEKIQKLS QRSSGAKHLV ENLSKSRDSV EEFVDMLKEN LSLLKEDIND
FVDKSESLKE TNIMYAYNST VESYRKSINA SRKVNESLYI FNQGDEMQYE VQDLLRIHKN
DFDKLFIENN AALILIKNKY KKLKENSYKL NKLICGGMSE TFECDVLCGG PTNVCPFCGG
EACKNGAVPN AVEAINFGNE AIEKLKQLED ITEKKMYELN ILQNIVNKTH RDVDKVINLL
NKTKNEYYDA GVVSDDIMEK IDEFLNKDRI SMENISNIIN EIDKMKIDID RDEIYKLTVN
LFSTVRTIPN VDEISREAIK NKTRAYEIME KARNSLKLSK GVLNDSRNAQ DIIKNVMENI
INIQSTINNF SNNIIEGRNN FYSGDRIAKK IDEELNEIKE YYNSLNKKFI DIKVNELKSN
TTMENAIDKD LKTQEIIKSI KVTAFDLKND IVKGYKVIEE KSRYGCGYLL ERAIPLRERA
INFIEKASTV EDEIRELENI IFDSEKDIES MMNEIDKETS IIDKNIEEYL YIEEHYENCD
F
//