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Database: UniProt
Entry: A0A0V0XA91_9BILA
LinkDB: A0A0V0XA91_9BILA
Original site: A0A0V0XA91_9BILA 
ID   A0A0V0XA91_9BILA        Unreviewed;      1671 AA.
AC   A0A0V0XA91;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   SubName: Full=Laminin-like protein lam-2 {ECO:0000313|EMBL:KRX84934.1};
GN   Name=lam-2 {ECO:0000313|EMBL:KRX84934.1};
GN   ORFNames=T06_2248 {ECO:0000313|EMBL:KRX84934.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX84934.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX84934.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX84934.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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}.
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:KRX84934.1}.
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DR   EMBL; JYDK01000003; KRX84934.1; -; Genomic_DNA.
DR   STRING; 92179.A0A0V0XA91; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   CDD; cd00055; EGF_Lam; 9.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 9.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000034; Laminin_IV.
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; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 11.
DR   Pfam; PF00055; Laminin_N; 2.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00180; EGF_Lam; 10.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 10.
DR   PROSITE; PS01248; EGF_LAM_1; 3.
DR   PROSITE; PS50027; EGF_LAM_2; 8.
DR   PROSITE; PS51115; LAMININ_IVA; 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:UP000054673};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..1671
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006872404"
FT   DOMAIN          51..326
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          327..385
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          442..488
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          489..541
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          568..741
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          776..824
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          875..929
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          930..985
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          986..1033
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1034..1080
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   REGION          1483..1508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1085..1112
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1568..1660
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        351..360
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        442..454
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        462..471
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        512..521
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        794..803
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        899..908
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        958..967
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        986..998
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        988..1005
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1007..1016
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1034..1046
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1036..1053
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1055..1064
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1671 AA;  185240 MW;  C4BFCC1A9F988934 CRC64;
     MKKKVSNSHG LTAMKLSHLT LIIFTVVSTS AQEELDEYPQ SSGRCVDENG VAQRCVPEFI
     NAAFNRPVEV TNTCGLSRPV EFCVQTGHSG MNKVCDVCDA RVSSQAHPSF YLTDFNNPNN
     ETWWQSETMA EGIQYPTTVN MTINLVVKFE IIALLHIYSN VNDCPVQGSL VIQYAWSDVA
     ISKAFDITYV RLKFRSPRPE SFAIYKKSRA DSDWSPWQYY SATCRSTYGV PEKAPILPNA
     EAVAQCSAEY SDISPLTGGN VAFSTLEGRP SAHNFEESSV LQDWVTASEI RIVLTRLNTF
     GDEVFRDIKV LRSYYYAVSD FAIGGRCKCN GHASRCVKST GHGEEKLVCQ CEHNTHGEDC
     DECLPFFNNR PWKAATAENA NECQACDCNG LSNRCYFDEE LYRMTGNGGH CINCAGNTRG
     AHCEACLENY WRAPGQQTCL PCNCNEIGSV NMQCDDSGQC ICKPGVGGQH CDRCLPGFYE
     FSALGCRDCG CLESGSLDNQ PSCRSDTGDC TCKRNVEGRQ CERCRPGFFN LDLENEFGCT
     PCFCFGHSSV CDSALGYYKS NITSTFDSSR DGWKAERYDG RETELQYNLM DQAVSVAEFD
     GPSYFIAPGK FRGNQRSAYN QILSFKLKVV QSNARASVRD IVLEGADGQV ISVPVFAQGN
     PVPASYEQIY RYRLHESADF GWTPSLSTTK FLGLLSNVTA LKIRGTFAAG DVGGLDDVIL
     QSASMTPNGE ELGQRAMWIE SCQCPDNFVG QFCESCAPGF RREPKFGGPF SRCIKCECHG
     HADLCEAESG RCICEHNTAG DNCERCARGF YGNALNGTVN DCIACPCPDS GPCLLHTDDD
     IICLDCPNGY AGRRCEICSD GYFGEPSNGR NCTFCKCSGN IDPNSVGNCD RTTGECKKCI
     YNTHGFECEK CLPGFYGDAL LEPKGDCKPC DCYSFGTYKP RTDYDFLECQ QNDGQCQCLN
     HVTGRRCDQC ENGYYNISSG EGCQPCNCDP LGSLNTSCDI NTGQCVCKPG VIGRRCDQCA
     MRHFGFGPKG CEACNCLVMG SVNLQCSITT GQCQCHPNIE GRQCDRCKEN MYNLEAGCLE
     CPPCYKLIQK YAKQHREKLD ELKDLLAEII ANPMVINDTN FEKKLAEVHE DVTKFGVEVK
     ERLAGGDSSL IKRVSKLRDD ITKAEESLAD VDHLLLETNF TISEAVNIMS SWDRIKEKSY
     AELRHAQYFL NNDAVEAWNR AKLASDRFGR PSEEMTNLAE EARQLAERQM NNSLTIERYA
     ADALNVSKQA YKKAHEAIYG SEAISSEISR LQKSYVSAEE LQNQTISMAK EQVDRAEQVY
     QKAAEMLNKV DSLKIPEVDI DGLQKKALVV SEEAKTVRSE AENLAMENKP VVDQVNRMRT
     HAEYELMRAE NQQQIADALL ADLDAAHAKA QKAVALAEST LLEANNTLRT LEEFDALVQQ
     SKLQAIEALA RTGEIESTIK EAEQWSSEAE LLLGNAKDDA KKASRIAQDA REDAEKASKS
     AEKIRSDAHS TKLGVQKLKV EAENVKADAN KATNTLNNYR MLSADDKQKA IEALELASQA
     DLLANRSNRT TTEAIETLKK ILNELNNLER VKQADLDMLA EGVAGATQVL SDANLEQEVS
     SLKAKQMEQQ RRINLYQADI DRLEREVRNI EQIRDSLPDR CYNVIDIEGS R
//
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