ID A0A0V0XRA0_TRIPS Unreviewed; 3186 AA.
AC A0A0V0XRA0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Laminin subunit alpha-2 {ECO:0000313|EMBL:KRX90427.1};
DE Flags: Fragment;
GN Name=LAMA2 {ECO:0000313|EMBL:KRX90427.1};
GN ORFNames=T4E_128 {ECO:0000313|EMBL:KRX90427.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX90427.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX90427.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX90427.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
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:KRX90427.1}.
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DR EMBL; JYDU01000166; KRX90427.1; -; Genomic_DNA.
DR STRING; 6337.A0A0V0XRA0; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00055; EGF_Lam; 15.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 12.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
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; 13.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00180; EGF_Lam; 15.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 4.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 12.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 11.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 67..314
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 442..496
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 497..545
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 566..747
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 781..831
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 897..948
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 949..995
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 996..1043
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1044..1093
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1094..1141
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1189..1234
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1235..1291
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1303..1502
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1692..1745
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2301..2484
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2499..2680
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2683..2872
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3002..3178
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1995..2022
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2246..2301
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 442..454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 472..481
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 516..525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 800..809
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 921..930
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 949..961
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 951..968
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 970..979
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 996..1008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 998..1015
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1017..1026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1066..1075
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1094..1106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1096..1113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1115..1124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1189..1201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1191..1208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1210..1219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1235..1247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1262..1271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1692..1704
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1694..1711
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1713..1722
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2653..2680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX90427.1"
SQ SEQUENCE 3186 AA; 355101 MW; 9F12644ED26AB159 CRC64;
LASSTRQAVA YTVKSLSNSM TGKLWAALLI ITFNFFTNAV DLSLTDFSDG DWASDDYYVA
EFSGSKNGRG LFPNIFNLAT NAIITANATC GEAGPENYCK LVEHVFMRSP QCDVCDNNNP
SKRHPIEFAN DGTNRYWQSP TIATGLQYEW VTVTLDLRQH YQIAYVIVKA AIAPRPGNWI
LEKSIDGIEW KPWQYFAYSD EACMRYYGVP AAAVVPKITR DDEVLCTSQF SKLDPLEDGE
IHTSLVNGRP GVDGPSDTLQ EFTRARYVRL RFQKLRTLNS DLIYITRKPK HEHIDESVTR
RYFYAIRDIS IGGQCICYGH AESCPADPVS GQLQCECVHN TCGENCERCC PLFNQKQWRR
GTTSDSGDCE PCQCFNHATE CRYDPEVEKQ HLSLTPEGIY EGGGVCIDCK HNTQGINCQE
CKDFFYRPTG VSVYDQNTCQ PCECDPLGSI DGSCVKEQST APEGMKPGDC FCKPGFGGKR
CERCALGYRN YPVCEPCPCS RAGSSNYATC EEDCICKENV EGIFCDHCKP GFFNLDEDNP
AGCTACFCFG MTDKCKEASL AKRTIIDMSN WTLSSLDGSK SYKPTYETFG GLSLTMDNRR
INDMTLVYWK APSNYTGDMI ASYGGNLRYY VYFVAERDGS HIPIADVVLK GNGLEIEHHV
DQPFYERENV TVTVKLHESW SWRDVKSKRP VSKVDFMTVL ANVELLMIKA VYRKSQLQSN
IHSISMEVAV AEATENNNSS LMKSVEMCEC PEKYSGLSCQ SCIPGHRRLN NILYKGRCEA
CLCNNRSLRC DAHTGHCLDC THHTTGARCE HCARGYYGNP QLQGGDSACK PCACPLLNPE
NNFSPTCISA EYGLAHSYSA DYICTECQLG YTGIKCEQCA DGYFGNPMVP GNFCQPCQCN
GNIDTAAVGN CHHRTGECVK CIGNTVGWNC ERCKDGFYGN ALENNCRACG CNLHGSLSLN
CDQSNGTCSC KKYFIGRQCD QCEEGYGDIE NGCLECACNE VGSLSLRCDP VSGQCPCKAG
VFGKRCDTCV SGYYDFSERG CQFCNCFAPG SVENGKCDLK TGQCVCLPNV VGQKCDRCQD
GYYNISSGEG CKPCDCDPHG SDDEVCDQQT GQCKCKHNVA GEKCDKCAPN YFGYVSHGCK
ECPRCPAPGH VCHPTTGECV CPPNTVGDMC EQCAQNSWNY DPLKGCEACD CNIDGSKSSV
CDLHTGNCKC RTGYTGQKCN LCMPGFFDFP VCRPCQCFLP GTDPNTCHSD GCTCDDQGQC
ACKKNVHGLK CDECQPYSFS LEEANPDGCT ECFCFQRTNF CIQSSFVWQQ IITEDRHAFF
VQPWLYPTRI HGLEVLPSEP LVLNSYPADH TPIYWSLPKR FLGDKILSYN GLLRFEVSNI
GNHFIDGSLK PDERLFEQYP LVVLVGNHRL VFEHYKSRFE ISPNGVYTVK LRQDQWKARQ
QKELPVSRQA FMTALQNLQA IYIRSTFNER IHEASLSGVT MDMAVYENTT LAGNKTAVGV
EACDCPKDYS GTSCQKPADG YCRKKHVNYL DSANELDLVG WAESCACNEH SSSCDRETCV
CLVSCLLIGV VVVVVVGRCC VSAHLVFVVC FVFSSLANTT PPAIIVNIVP SAITAMQRKE
PRMIVENALV RVWIRVSASR VIRLLRAKDT RAISANPATL ESIANSREPQ RMFCMYGYFG
DPQREGGQCT ACDCNPYGSL SEICDSISGQ CQCREGVTGR DCSECQSRYA LVGAECQSCD
VGCTKELMAD ADQLNAVIQT VNISHFIPAP WGRALRLQND TDNMRRQLQS ILQARLDAEQ
ILLDLSDGDE FTNQVDSLQK DVTYLQEKTI SSKAKAAQFM NNSEHVTTDV RSTLEKAFAL
RQALLIYLAS ASDASQEELT EWLEQMKQIL DEIRGRDEYL QKHLSRAEME LRRQKELLAV
VLAKKFNDTQ FERLKEKITA ETKRWENMRD IIWDTVRKQS TSASATLSTA TKMLQQYMNI
LEDVETIGQG SMKVLADAQE KLDNATQDLL NVHDNYREAN QSIPRLEEAL VLCDKEASRL
AVLLPGHREK YYYPAESHAD MLEVEAAEIK NSFAETKDAS HLALVASGVY ENIVEALQNA
SKAADLAQEA THRTDKLISN PEYPLVDSAR QVTNHSMELH KDAQLIDVNG LLNKVTEYEN
RSSGMKSNID DSTKDLENIW SSFDKFDDFH NKMEGVHDIT KKVSKQSTAE EGQTSAVIDS
VTSLGNKVKE FLSLTSLGIR KVTDSVNRSL EEVLRARERL NRVRTQADNN DQKVFDLNNK
LSLLKEKIKE AREKASKVKL SVKSNVDDKC FRSYSSPMVP SISNEISVAY RPLDRVPNSL
LFLTQTERTR TQNTEYMAIE LRDRQIVFLW NIGGGDQKVT NLKQIRSVAR KDRIAWYTID
VKRNGNAVVL NVTDDEGSTT VHYDGGGSHA VFNAIPGRTT LSFGADPSKL PPTISTSQFR
GAVGRVEVDG HAIPLWNFNA DEHCVGNFPK TSTKPLEGLV QGWMFRDGYA QVAPNSLLYD
MREFRIQVNF ATYSETGLLY FRGDPKTKDF VSIELKDGHI VLQFYLGGLS KLRLVSQHAY
NDGKFHNVLA LRMKTNGTLR VDSDSDVVTG EAAPGSTGLN IRDHDHYVGG VPDSFPKDAW
FSYGIQWRGF YGCIRSISHG FGQNIDIRNA LKSLNVDESC VESNERLATD DRVISFNGQG
VFAMQSFILD EDSSLSFNVR TTAEEAILLY QSSQLKNKRR RDIHSEGFIV VYIMQGRVYV
HIGRSTDSAI TLHTDDNFND GKLHNILIKR EKTSVTLFVD DLEMDSGEFD TLWTLGSVES
ILLLGGLAGV KVPSDEATVT RSFVGCLSDF FLNYERMPLL PHFLLNARLG YCGLGSYDSY
YGVKSMDPLL ADDSTGQIPV LFRKRLWPAL SAKKNGKKWQ LKSRRGAYVD FAFGLGERIT
SSTVASTSEE IESQLTTTTT TTTITSGSGV APVFTTEAPI FSSGELENCK LSPCCIGKPV
QNALFYNSTA SYTRMFFQEN IADAGDLKFS FHFCTAGPDG LLLFWSNRKY SHYVALVLEN
GLLTLHLQGH KMISPIMATV TSGRRLDDGH WHRIVFNKQQ KQLSIQLDHH KPTFLKKLPK
TLTLRMAGGL LLGGLPKKIQ NRIQTKFALP FIGCIGDFEF NDKSYALING RNQMTFSCRQ
VKKIAS
//