ID A0A158RC97_THECL Unreviewed; 1797 AA.
AC A0A158RC97;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Laminin subunit beta-1 {ECO:0000313|WBParaSite:TCLT_0000683601-mRNA-1};
GN ORFNames=TCLT_LOCUS6825 {ECO:0000313|EMBL:VDN04221.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000683601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000683601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN04221.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; UYYF01004448; VDN04221.1; -; Genomic_DNA.
DR STRING; 103827.A0A158RC97; -.
DR WBParaSite; TCLT_0000683601-mRNA-1; TCLT_0000683601-mRNA-1; TCLT_0000683601.
DR OMA; TDICREY; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
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: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; 9.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR PROSITE; PS01248; EGF_LAM_1; 6.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1797
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041162299"
FT DOMAIN 34..275
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 344..406
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 407..466
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 467..517
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 557..771
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 777..824
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 825..871
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 872..921
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 985..1036
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1037..1087
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1144..1190
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1232..1259
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1443..1477
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1624..1651
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 374..383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 437..446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 489..498
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 501..515
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 777..789
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 779..796
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 798..807
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 825..837
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 827..844
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 891..900
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1009..1018
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1060..1069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1144..1156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1146..1163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1165..1174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1797 AA; 200974 MW; 2587ADE4B02430A0 CRC64;
MRFSESAAQF ISLISILLLG SSFEYESAEE DICNERSCYP ATGNLLIGRK KSLTATSTCG
LRGRQRYCIV SHLEEQTKCF YCDSRTEWKP NREPYKLSHR IENIVSESYE DRHRNWWQSE
NGVQNVSIRL DLEAEFHFTH LIITFKSFRP AAMIIERSAD YAKTWTPYRY FAYDCQSTFP
NIPEGPPKKH SDVICTTRYS DVAPSTGGEL VYKVIAPHIP TENPYADEIA NLLKVTNIRI
NFTKLHTLGD DLLDYRPEID EKYYYAVYEL VIRGSCSCYG HAQRCIPIDS SARISIPYRA
DMVHGRCECT HNTKGLNCEQ CMDFFNDLPW RPAIGDDSHE CKRCECNGHA ARCHFDRAIY
QASGFISGGV CDECMHNTQG KNCEQCKPYF YRNPERPITD PYVCLPCKCD RAGSLNDGIC
EGEEDLERGL VAGKCYCKPN VEGSWCERCK NGFWKLTEED PNGCRPCSCN LFGSFNNEGC
NKKTGECLCK RLVTGDACDM CLPEHYGLGD DPNGCKPCDC DLGGSVDNNC DIITGQCTCK
ENFVGRRCEA AESAYYCPSI DHFTFEAEKA EVAGGEIEFR EFATNGRHKT WTGDGFVRAN
EHTRMVFKIE GIAQSMHYRI VIRYELLQDN IGWENIQLTV VRPTDLLPDR VCKNLSPSDD
FLIARLYPSL HYIEIMPDVC LQAGIPYEIH MQMGEKRSGI NDRTATVLID SIVLIPSTEE
LFISQRISTD NQHKMEYDRY QCREQQLSLI PMLDLSDVCV RYICPIAAML FNRSLDCECD
PTGSLSGICS GKGGQCDCKP NVVGRRCDKC AVGTYGFGPS GCTPCECDSV GALNNICDPQ
SGQCNCRENG ITGRQCSQCQ PGFWSFPDCH LCQCNDHASV CDQQNGACIE CRDLTDGYYC
DRCKDGYYGD PRLGINLPCK PCPCPGSLDS GFQHADTCYL RTSEFSETPD VICNCREGYI
GERCSSCALN YWGNPNELGG SCEPCDCNGN IDVTVEGSCD AVTGDCIKCL HNTEGVQCEY
CSRGYYGDAK IRSCQRCVCN ELGTNKTIEF CNHITGQCPC LSNVVGKECD ACAPHHFNLA
SGKGCEPCGC DPTGVILDND GAPDLHCNEL DGRCYCKPGR GGRTCSDCEN YHWGDPARDE
CRKCECNIIG SATQQCDRSN GHCVCLPGSG GPLCNICARG YTGQWPQCEA CGECFHNWDE
IVQNIKSQVN NLIGATKNIE DTGIASVYDD QFEKMEKILA NLKIQLESAN ITRIDINKQQ
NEIGKLRRDI TLKKEFLNRV GGHITEISSD VDQADLELKS LLGEVEKLAL KSQTFKKNAT
LLRVTDVQGA YNITRESAEK SSAARQRTDE ANFKITDAES FRQRAIQLLD NNRLDFEKQF
DENDVALVQI DKQLAKLESI MPKLNKDVCG AESVAFCDEL CGGPGACGYC GGRSCLSGSV
SKAEIAKKFA DEADQKLEEK QKEAEKILGR IQEILLQISL IKSEAKSGHD AAEIAALQVP
VQANQIRTTM EEMLVKMNHF IDNNQRYNPE QIQALVKVIT AATISLTPVQ IEKLSKQIRE
KLQNISNTDM ILNETHSSKA IAEALQKSAA LANMRATKIR NTTTVVREAL KKASLAQNIA
RDAMKKATER IMGARNDLND ATNQLEFAEI SATKTNQSLM KLDNDMKDIN VQYLSISEDT
KYAYEAANKA IRQVEYAEAA KKKLKVSFEQ TKELLLSQNI DNELPQERAE ELRKRATQLL
HKTQRHRSDI LQLSTNIDAF DVRLTDYVLE TSELHSRIDT VTAQIHKQID YYSACDI
//
