ID A0A0V1BJU1_TRISP Unreviewed; 1694 AA.
AC A0A0V1BJU1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Laminin-like protein lam-2 {ECO:0000313|EMBL:KRY37068.1};
GN Name=lam-2 {ECO:0000313|EMBL:KRY37068.1};
GN ORFNames=T01_12246 {ECO:0000313|EMBL:KRY37068.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY37068.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY37068.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY37068.1};
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:KRY37068.1}.
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DR EMBL; JYDH01000037; KRY37068.1; -; Genomic_DNA.
DR STRING; 6334.A0A0V1BJU1; -.
DR eggNOG; KOG1836; Eukaryota.
DR InParanoid; A0A0V1BJU1; -.
DR Proteomes; UP000054776; 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:UP000054776};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1694
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006875232"
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 591..764
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 799..847
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 898..952
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 953..1008
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1009..1056
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1057..1103
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1506..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1108..1135
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1591..1683
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 817..826
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 922..931
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 981..990
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1009..1021
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1011..1028
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1030..1039
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1057..1069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1059..1076
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1078..1087
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1694 AA; 188118 MW; 571FC9EEB75168E1 CRC64;
MKKKLSNSHG LTAMKLSYLT LIIFTVVSTS AQEELDEYPQ SSGRCVDENG VAQRCVPEFI
NAAFNRPVEV TNTCGLSRPV EFCVQTGHSG MNKVCDVCDA RVSSQAHPSF YLTDFNNPNN
ETWWQSETMA EGIQYPTTVN MTINLVVKLE IIVLLHIYSN VNDCPVQGSL VIQCAWSDVA
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 NITSTFDSCN FILFFAFLNY YYYPLFVLMY TARDGWKAER
YDGRETELQY NLMDQAVSVA EFDGPSYFIA PGKFRGNQRS AYNQILSFKL KVVQSNARAS
VRDIVLEGAD GQVISVPVFA QGNPVPASYE QIYRYRLHES ADFGWTPSLS TTKFLGLLSN
VTALKIRGTF AAGDVGGLDD VILQSASMTP NGEELGQRAM WIESCQCPDN FVGQFCESCA
PGFRREPKFG GPFSRCIKCE CHGHADLCEA ESGRCICEHN TAGDNCERCA RGFYGNALNG
TVNDCIACPC PDSGPCLLHT DDDIICLDCP NGYAGRRCEI CSDGYFGEPS NGRNCTFCKC
SGNIDPNSVG NCDRTTGECK KCIYNTHGFE CEKCLPGFYG DALLEPKGDC KPCDCYSFGT
YKPRTDYDFL ECQQNDGQCQ CLNHVTGRRC DQCENGYYNI SSGEGCQPCN CDPLGSLNTS
CDINTGQCVC KPGVIGRRCD QCAMRHFGFG PKGCEACNCL VMGSVNLQCS ITTGQCQCHP
NIEGRQCDRC KENMYNLEAG CLECPPCYKL IQKYAKQHRE KLDELKDLLA EIIANPMVIN
DTNFEKKLAE VHEDVTKFGV EVKERLAGGD SSLIKRVSKL RDDITKAEES LADVDHLLLE
TNFTISEAVN IMSSWDRIKE KSYAELRHAQ YFLNNDAVEA WNRARLASDR FGRPSEEMTN
LAEEARQLAE RQMNNSLTIE RYAADALNAS KQAYKKAHEA IYGSEAISSE ISRLQKSYVS
AEELQNQTIS MAKEQVDRAE QVYQKAAEML NKVDSLKIPE VDIDGLQKKA LVVSEEAKTV
RSEAENLAME NKPVVDQVNR MRTHAEYELM RAENQQQIAD ALLADLDAAH AKAQKAVALA
ESTLLEANNT LKTLEEFDAL VQQSKLQAIE ALARTGEIES TIKEAEQWSS EAELLLGNAK
DDAKKASRIA QDAREDAEKA SKSAEKIRSD AHSTKLGVQK LKVEAENVKA DANKATNTLN
NYRMLSADDK QKAIEALELA SQADLLANRS NRTTTEAIET LKKILNELNN LERVKQADLD
MLAEGVAGAT QVLSDANLEQ EVSSLKAKQM EQQRRINLYQ ADIDRLEREV RNIEQIRDSL
PDRCYNVIDI EGSR
//
