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Database: UniProt
Entry: A0A0V1LLL1_9BILA
LinkDB: A0A0V1LLL1_9BILA
Original site: A0A0V1LLL1_9BILA 
ID   A0A0V1LLL1_9BILA        Unreviewed;      2026 AA.
AC   A0A0V1LLL1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Latent-transforming growth factor beta-binding protein 2 {ECO:0000313|EMBL:KRZ59950.1};
GN   ORFNames=T02_11231 {ECO:0000313|EMBL:KRZ59950.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ59950.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ59950.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ59950.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-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:PRU00076}.
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:KRZ59950.1}.
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DR   EMBL; JYDW01000035; KRZ59950.1; -; Genomic_DNA.
DR   STRING; 6335.A0A0V1LLL1; -.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 4.
DR   Gene3D; 2.10.25.10; Laminin; 15.
DR   InterPro; IPR006150; Cys_repeat_1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001507; ZP_dom.
DR   PANTHER; PTHR24039; FIBRILLIN-RELATED; 1.
DR   PANTHER; PTHR24039:SF28; FIBULIN-1; 1.
DR   Pfam; PF12947; EGF_3; 2.
DR   Pfam; PF07645; EGF_CA; 6.
DR   SMART; SM00181; EGF; 21.
DR   SMART; SM00179; EGF_CA; 14.
DR   SMART; SM00289; WR1; 2.
DR   SMART; SM00241; ZP; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 8.
DR   PROSITE; PS01187; EGF_CA; 5.
DR   PROSITE; PS51034; ZP_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1995..2016
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          440..474
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          477..515
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          516..556
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          654..692
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          999..1041
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1042..1082
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1607..1646
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1647..1688
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1702..1938
FT                   /note="ZP"
FT                   /evidence="ECO:0000259|PROSITE:PS51034"
FT   REGION          1578..1601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1581..1601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        443..453
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        464..473
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1010..1027
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   2026 AA;  224124 MW;  9BACBCFAB77E505D CRC64;
     MTSRNEIYFQ NKFKNLQNDL KPLNNYLHLS ACDSTKSANT PRWKYSLNKY ATKETLVNKK
     PLSPVTNIAL VDRKKEQYPR MPVTNFEDEY YSNQISDDYV KLIRYGYKSD AQVQLNANLS
     DFQGKNVKFP SAENVHVDLL NTPQGSNFYG DNARKKMFST FPSEKKERKL FFSNSRCFKT
     QLVNPTPINP LLRAKSVNSI DAEIKFANKD DTKKDLFNIN NRLLFSDSGR NLNNDGRELS
     KQYAILQKMY HDWQDVVKGH EEIRVQGKKL NNEAVENFKN FQLAMLHQLN IVQELCNEFL
     QNEKSDIKNV TKSCSDQSTF ENSDSSPPNK VDSLSKISSY KMYRLFLNGR YPSSSDGFYL
     LYLSFLEIIE CDRWQSSSGA KEVLHHKSTS IINFDLSLVV CQSSENDQQL AIFPISGLCN
     GRAQCFNDAV IKEDQFTFCS NECLPKCGPH GACLKVGQKA RCFCDNGYSG KYCTIQEPNE
     CASRPCHFLA QCTNATGIFG CSCLDGFEGD GYNCTDINEC ELPSKQPLCP ENSVCHNIPG
     SYFCDCATGY KSKNGLGGMC EDIDECEDKT HNCTSLEQCI NTDGSFRCES RPCEIGFEKI
     NGVCHDINEC KTSNACSPDQ SCINLIGSYK CIDQISAGQS KSTSKIDEID ACLVNESCVK
     NASICHDRAV CLSQVDKCAC TTGYEGNGIH CIDINECAKD KYICPSETNC INLDGGFTCC
     DSEKSKEECL KTKHIICKSD NECRSNSKCI DHHCKCQQGF HLNENLECID IDECSSFSTI
     CPEKNWCVNL PGSYVCCNDT ASVSQCLGII IYAPVQKGST LNKKISAGSS SQQITVVPLP
     DVKTTPIPQY HTDMVYITPD TEISSSSLNF EEFNSGDKVT NELTDQNFGS GLGSGSGEIS
     VDLLSSASPN TAEITSELIS ELNTASTERP DLDYEQTEGA TESIQSTDST SILENKKNIE
     DENDKSLTTA QVDSSIRMES EETIDEIESE YVRPAVDYFE KKCLLNESYC HYHAKCLKAN
     FSDEFVCACD AGFQGDGYHC EDVDECIYSD KICSPLATCV NTIGSYKCIC KPGYAGNGTF
     CSPLCPRGHK PLTTRCSLEE NGQTCTAGYT CIHGFCCPSQ SAQEEDCSLD PTICHESASC
     INKVCQCNTG FEGNGYICKD INECALHLDN CVPPLRCQNT IGISRYCSIL RPSCGPNAYC
     RNNRCACKDG FILDNNACVP DPNNCSSNRM LCDPNATCIN GKCTCSAGYI GDGLKCYPDP
     QDCHNNVSLC HQFARCIDRR CECIPEFSGD GITCFPNPVP FYKNCTINPS VCPTEAQCYY
     GRCVCKVGST NLCNKTNLVI INEKNDCRMD PSICHTNAVC RKGICICKKG FIGNGFSCMD
     DPNDCLKNKG ICSPNAICVL RRCKCKAGYV GNGISCVPSN QATTCSSNKD LCDVNAECIS
     DKCVCREGYL GDGMHCSADK EDCIINPSLC SANAQCISRR CVCQSGFIGN GKTCNESKSD
     PSSQKNKCEN CDFNAVCEDN KCQCKQGFEG NGTLCYNNAN IRCDDDAKVC GIHATCISFG
     TKMVCICNKG YTGNGRDLIK STTEPNKEKE NGSKETSTLQ EKKEEKSDNL CDSVKCGPNA
     ECKINMSGLP ECRCSRGFTG DGKECYDLNE CMLRISKCHH LATCVNTIGS YVCQCPDGYA
     GDGVRVCSRE IKVSNLNYID TICEKNGITL QMTNRSDLYG KVYVKSQSEN PDCSQTLPKK
     LNNSFKFTAR FEKCDFKKEA EDTYSVIMVI QKHPSFITTG DEAYKLVCTY PSAEREVHES
     LSVETLNSSA SYVEKSVGSK CILDVVDANT GKAITEATVG QKLQMKLRAE SSGNYELYGT
     NCVVINMETG ESFALTDEDG CAVEEEIFPN WKKMGNSLYS EFITFKWPET ATVRFQCDCS
     VCAHQCPERK CNSKLKSPKK RSTTSTSNAI NNQNYVQSNI LKIISDGNLE SEVKLDEIID
     WDNYDNDKIC VDGTIMSALF GFGVIFLVAA LCALFFKQLA NIRNDI
//
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