ID A0A443SH30_9ACAR Unreviewed; 1906 AA.
AC A0A443SH30;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Laminin subunit beta-1-like protein {ECO:0000313|EMBL:RWS26837.1};
DE Flags: Fragment;
GN ORFNames=B4U80_08952 {ECO:0000313|EMBL:RWS26837.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS26837.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS26837.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS26837.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS26837.1}.
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DR EMBL; NCKV01002434; RWS26837.1; -; Genomic_DNA.
DR STRING; 299467.A0A443SH30; -.
DR EnsemblMetazoa; LDEU005203-RA; LDEU005203-PA; LDEU005203.
DR VEuPathDB; VectorBase:LDEU005203; -.
DR Proteomes; UP000288716; Unassembled WGS sequence.
DR CDD; cd22302; cc_DmLAMB1-like_C; 1.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 11.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
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:SF435; LAMININ SUBUNIT GAMMA-1; 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; 6.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 12.
DR SUPFAM; SSF57997; Tropomyosin; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 10.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000288716}.
FT DOMAIN 186..426
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 488..550
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 551..609
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 610..660
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 700..900
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 906..953
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 954..999
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1000..1049
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1109..1160
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1161..1211
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1212..1259
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1260..1305
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1364..1426
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1585..1633
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1709..1893
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 518..527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 580..589
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 632..641
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 644..658
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 906..918
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 908..925
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 927..936
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 954..966
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 956..973
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 975..984
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1019..1028
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1133..1142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1184..1193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1212..1224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1214..1231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1233..1242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1260..1272
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1280..1289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RWS26837.1"
FT NON_TER 1906
FT /evidence="ECO:0000313|EMBL:RWS26837.1"
SQ SEQUENCE 1906 AA; 214034 MW; EA0312EBE8EE2850 CRC64;
SETAHSRSSE PKIVEGSYFD QRRNFDQRRT PYSLEGISHR PDSSRRTEYE QGSYGRNYEY
SSSRDTTRDS YRGGQYSRTY NRTVVSNVDS VRQPVSSSSH ITRQYNTSIS QGSRVTSISS
SGQRVHTPLL WYNRTWHWST NKTRAYDADL DGTTLPPNSF DPIFENTVHK FDDNHPFNKF
GQTSCDSYSC HPPVGDLLIG RENKLSASST CGLYGPQKYC ILSHLQSRKK CYTCNSDDRY
KDDNYQYHKI QNIVTKEHIR NEKFWWQAEN GVENVSIRLD LEAEFQFTHL IIVFQTFRPA
AMIIERSDDG GNTWKIYQYF AKNCKETFRH VKMGPRRKVD DVVCEQKYSD VNPSSNGEVI
FSVLPQHIQQ QINNPYSEEV QSVIRITNLR INFTKLHTFG DDKLDNREEI KRKYYYAINN
MVVRGSCSCY GHASRCISEG HVVPGMVYGK CDCNHNTQGA NCEKCKDLYN DLRWKPANGS
ETNACKKCNC NNHATRCKFD EAVFQASNGV SGGVCEDCQH NTEGKNCEFC KPLFYRDPQR
SIDDPNVCQP CDCDPRGVLD EGNCDNLDSD YSTVAGKCRC KDNVDGRRCD RCKPDFWNLN
KSDPLGCLPC TCNKNGTVGN MGCNPTTGEC ICKRNVVGKN CNECAPDHFG LREEDEGCTP
CDCDVGGSYS RSCDVRSGQC SCRPYLKGRT CRQIEDNFFV PDLDYLTLEG ENGRSDAQSQ
IIIRQRYPGQ EPTWTGDGFR EMYPGSFIEF DVSDIPMGMD YDILVRYEPK PERVEAKVVI
DSRGQSFGTC RNKINDRGTV NLEPHYRVAT VSGGPFCFEK GGHYKVKLEV GPSTDISSIL
VDSIVLIPDV HSMDILNTPN AKREFDHFKC GQLFNSAATR PHTIPEVCKK YLHSITMQVF
DGARPCDCYP LGSKSLICSK FGGRCECKPN VVGLRCDRCA NGFYDLGADG CKPCDCDSVG
SLDNLCDQQS GQCKCKNNTY GRKCDECQPG YWNYPSCEKC RCHGHTERCD SKTGICINCR
DHTAGPHCEI CEAGYYGNPL YGPDNQCKPC PCPGLPGSSM SHADSCYMDP RTGIPVCRCH
PGYVGDQCDK CAENYWGNPS VPGGKCLPCD CNNNIDISQP GNCDQRTGEC LKCIYHTEGP
NCERCVDGYY GNATRQQCRQ CICHSLGTDK SKGSCNRTSG ECHCLPGVNG TQCDVCKENF
WNLASGKGCE PCNCDLQGSY KQKCDELDGM CHCLKGYGGK RCDECEPNYY GDPTEKCYPC
DCNTPGSATT QCARNGSCIC RKGIAGERCD RCARGYYGNA PHCQFCGECF ENWDMIIQNL
RNHTLRLLET AKRIRNTGTT GAYKEQFLTI EEHLLEIERI ISGASITEND IADIESRINE
LRNILNDLQD KLNNYEKQMD KTISRTTDAE INIADLRIRV KQLETDTIML KKNMTELQAM
NVDGAYNLTK QAQSRSRVAE SKVQSEVPML AQSEGLRRQT EKLLDTAAIH FNQSYNQNQI
AVAEIQRKIG ILEMDVPNVN ELVCGGRSTL DDCDSSCGGA LCPICGELSC DGAVTIAGTA
LEFGKKADES LKGLREFVNK QWNSIQDAKS KADEAYREAL NAYNKAMHAK SESENTTKDI
QDLLDKIDEF LDKALAKPSE IRTLANECIA KDISLTPTEI INLARQINET ILSITNIQKI
LLDTAGDLAT ANQLRQRADL AKIRADSILN TAKQVIDILQ RALEAQQKAE EAIRRATGNI
DNTQKDLDLI SQETAAAGKV SQGAQQGIAD LQKRLDELKK LYTSNELYVE KVVKESELAG
TMAKDAENGA RNLETKFEDA ARQLEEKANV SARVKERAEN LKERARLLAE NANSKLQDLQ
EIEDEFDENE RKLKSYEKLI DDLNRDMTEH LKTIDYWANY HRSCNG
//
