ID A0A158QQW9_HAEPC Unreviewed; 1784 AA.
AC A0A158QQW9;
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 alpha-2 {ECO:0000313|WBParaSite:HPLM_0001606901-mRNA-1};
GN ORFNames=HPLM_LOCUS16061 {ECO:0000313|EMBL:VDO58702.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001606901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001606901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO58702.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO58702.1,
RC ECO:0000313|Proteomes:UP000268014};
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; UZAF01019253; VDO58702.1; -; Genomic_DNA.
DR STRING; 6290.A0A158QQW9; -.
DR WBParaSite; HPLM_0001606901-mRNA-1; HPLM_0001606901-mRNA-1; HPLM_0001606901.
DR OMA; NCHACAC; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
DR CDD; cd00055; EGF_Lam; 16.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.10.25.10; Laminin; 17.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR PANTHER; PTHR10574:SF448; WING BLISTER, ISOFORM B; 1.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 19.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00180; EGF_Lam; 18.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 12.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 12.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
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:UP000268014};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1784
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041120291"
FT DOMAIN 37..281
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 362..416
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 417..506
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 507..556
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 577..729
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 779..829
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 948..993
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 994..1041
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1042..1091
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1092..1139
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1187..1232
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1233..1289
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1301..1499
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1543..1592
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1650..1696
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 362..374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 392..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 482..491
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 527..536
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 798..807
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 948..960
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 968..977
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 994..1006
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 996..1013
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1015..1024
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1064..1073
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1092..1104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1094..1111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1113..1122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1187..1199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1189..1206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1208..1217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1260..1269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1562..1571
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1650..1662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1652..1669
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1671..1680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1784 AA; 196566 MW; D018AEBB4B0C6781 CRC64;
MWPYSPLDWL LAIAVLVALA TCQDDYDPYQ EFIATESERG LFPSIFNLAT NSLINASATC
GYTRREEYCK LVEHVLLRKT AAGGSPQCDI CDANDARHRH PIEFAIDGTR RWWQSPSLAN
GLEYEKVNVT IDLRQEYQVA YVVVKMGNAP RPGTWVLEKS LDGIHYEPWQ YFATSDAECM
RQFGVPATTG VPRFERDDEK FTRARFVRLR LISPRTLNAD LMIINRQTHR IDRSVTMRYY
YSISDISIGG QCICYGHAES CPSDPVTGQF KCECRHNTCG ESCNRCCPLF NQLQWKPGTN
AHPNACQQCQ CFNHADSCVY DEELDRNKWS ITPEGVYEGG GRCVDCKVIF SGKVLEDACR
TCDCDLTGSV SDVCIRDDQS ALSGQHPGDC VCKPGFGGRR CERCARGYRN YPKCEPCPCN
QAGSVNFDTC EEEKCQCKAN VEGLYCDRCK PNTIHLSADN PQGCQACFCF GMTGQHPGDC
VCKPGFGGRR CERCARGYRN YPKCEPCPCN QAGSVNFDTC EEEKCQCKAN VEGLYCDRCK
PNTIHLSADN PQGCQACFCF GMTDKCREIP WVTASISNNV GWNLTDLSGG RDVRPEVENR
EVLMFNANQN KDRSLFYWKA PDTFTGNMLN SYGGNLQFYV YYVPLEQGNS IPVADLVIEI
PIREGSGWYN SVTRTPAEKV DMLRALAGVE RFMVRAMYQQ NQLQSSIFGL TLDTAVPPPE
GSPVDRIEDV LHPSMTDTRM RGVEVCQCPE NFAGNSCESC VPGYRRVNNQ LYGGHCEKCT
CQDHSDTCDP FTGACTNCQH NTTGPRCELC LPGHYGNPSL GGELGACRPC ACPTAENSRS
AECVMTQLVV SGPAASQEDA YVCTACERGY EGNKCEVCAD GFFGNPMEAN GTCKECECNG
NIDLMAIGNC DTVTGRCLKC IGDTTGEHCE ICKENHWGSA LEHTCKPCGC HHVGASSPQC
GNLGECTCKP NYIGKQCDRC IDGHGDIENG CPPCECDVVG SIGDQCDAVS GQCTCKQGVF
GKRCNQCRPS YFNFTDAGCQ FCHCNIYGSI QDGKCNNITG KCECRDNVDG TMCEKCADGF
FNITSGVGCQ ACECDPTGSD GEACDLHSGQ CVCKPGVTGL KCDRCQPNHY GLSPEGCKEC
RACPAPGQVC DPVTGECVCP PNTVGEMCEN CTENAWDYHP LKGCKLCECS DVGSSDGKCD
TRTGQCKCRN EYVGLRCDRC THGFFGFPNC QPCDCQPDGT DPLQCKDGLC LCNEEGECPC
KKNVMGAKCD QCKESTFSLE ASNPLGCTDC FCFNRSSSCE QSSLLWQQTY AEDRRAVFEE
PWEYYTKKHN LNLLKEYPAR YNSYPTDAVP LYWPLPKSML GDRTSSYNGF LRFKIWNEDN
RRGIDGVRPD TQYFRYFPQV VLVGNNRIEL EHIPLQIEED GKYKIRLHES EWRSRQSPEL
PVTRKLMMIA LQNLQGVYIR GTYNYPARGD AITMSEVSLD VAVPASPGLS GSTAIGVEQC
TDCPQGFTGS SCQNPAVGYC RKRQRDYLNS PDDMSLIGWS EPCACNGHST TCHPETCVCT
DCEHNTTGDH CDLCKSGYIG DAREGGANAC TKCACPLVEN SFSDTCVAVD YGRGYVCNAC
KAGYTGQYCE SCVIGYFGEP STPGGFCQSC DCHPDGSLNG ACNPLTGQCE CREGVTGRDC
SRCQHRHAFI GGVCTSCDQG CYLPLMTMVD DLEMTLANQN FSNLRPIPWK RLFRIENNTE
LIFDFMKGLD GGGESEVDAI VMESKHAKEA LAVVDGVSDA SKTF
//
