ID A0A077YVM5_TRITR Unreviewed; 1739 AA.
AC A0A077YVM5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Laminin G 2 and EGF and Cadherin and Laminin EGF domain containing protein {ECO:0000313|EMBL:CDW51826.1};
GN ORFNames=TTRE_0000008501 {ECO:0000313|EMBL:CDW51826.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW51826.1};
RN [1] {ECO:0000313|EMBL:CDW51826.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW51826.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG805810; CDW51826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077YVM5; -.
DR STRING; 36087.A0A077YVM5; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 7.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF310; STARRY NIGHT; 1.
DR Pfam; PF00028; Cadherin; 7.
DR Pfam; PF00008; EGF; 3.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
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|ARBA:ARBA00022989};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1739
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001728175"
FT DOMAIN 135..239
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 240..350
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 351..457
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 458..557
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 558..647
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 648..750
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 751..850
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 851..958
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1173..1209
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1227..1408
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1411..1447
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1582..1617
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 1199..1208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1437..1446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1607..1616
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1739 AA; 193958 MW; DACAA812BAEB7D72 CRC64;
MNFIAALAIS FFCQLPAIFC RLNRHIFYET VTLKNQCQSA DDAVWPHFES WLKVQTLGKS
ILWHQFGSLF VRHGNLYFKK LICLDQPLEQ TLNGAIYSSF SFYQPFLVTI KFVPPQTRSR
RRRHFHRKAC ELFLNQSRYE VDILEEVEPP VHVLSMRNHR AAGSFAVFSL TGVNNLQSSS
LFAINRTSGE IFTTGRLDRE QVDRHMLRVT CTEVSHPKQA AVAIVIVSVI DVNDHNPIFE
QSNYATMISE AVEPGTSVLH VHAHDEDIGP NGQVEYHIAP GQGSASELPF MLGADDGVLR
VQKPLDRETC AFYRLEVNAC DRSLPVTSRR CSKALVEVTV DDENDNAPQF EMENYYVEIN
EDVDFKIRPV ITQVVATDQD SGENGQVRYS IVSGNADLRF SIDYITGEVR VVDKLDYRQK
NHYELLIRAQ DGGHHSRSNT TLLGIRVLDV NDHPPRFYTT LFQESVKEDV PVGHRVLRLI
AHDPDSGNNA EIRYSISPQL NLDEVSGWLS VAEPLDHEVM PRIEFTVRAR DMGQPSLHST
ARVIIHVLDV NDNPPSFLEK FINVSVEETS PRGKRLLQVK AYDPDGSDSR LDYSIVSGND
DRMFILLNDE NNESLYFLGL KVTDNGGHSD TMTVQVQVLD VNSPPTFSEQ AISVHISEAE
PVGSIVTVVR AVDMDDGENA KLNYTMDTSS EYFSTDPETG VISLIHPLDR ENNSKFDLKI
SATDNGSPPL SCQIEVEIMI DDVNDNAPRF VDSVYRVSIS EDTPGGASLI QLTAVDADYG
LNSRVEGNEN NTFHIDANSG VIRLAYSLDR ETIAIYNLTA IAVDKGQPPL LGQASVIVTV
TDVNDNPPKF QQDQYQFDVK ENTPRGTVIG HLLAEDPDEG SNAVMVYKIF GGEDAASFEI
HSTETETLGV DVLTRTDLDF ESDQRTYHFY VQASSDELSS ITEVIIRVLD VNDHAPVLND
FNVVIYNYQW NGLVGRVPAF DLDINDTLRY RIISGNEAEL IELDESNGNM RLASHFSDGI
NKVEATCTLI VETITDKILL NSITLRALGV TVNALLTPLA YGRLVDAVAT LLPSNRQDVL
LFSFKQDEEI GTEPVVNISL ALRKSGTPLE ENFCVREPCI NYEACRSVLK FSGANDLIVT
ESFVLRPIHT VTTFLCECPK GYSGEHRSEC NIEVDMCFSS PCRSGGTCLS TENGYVCQCP
EDFTGKNCEL PIANSYCIPF LCRGGSSCEI VNGRQECKYC PHPERCMRFV LLLSEFSTNR
PDGLLLYAGC NKIDMDFLGL ELSEGRIKAS FSLGEEVRSV ILKSEQTVND GDWHKLELRL
LNQVFRILLK LYSSQCAAKV HANLEKKCVD QTISCYRFLD LSSPLYVGGL PQRNKQKRFT
GCISDLHIDH NLIDMDRYVD NHMTTAGCSG MKAYCEENPC LNGATCNDRL NTYSCDCAAD
FSGRNCSYGK LTIYLSSYVS YNLSERISVP FVFGIDFRTS QPDAHVLTAE LQSGQQLVLS
VCFVSGLHHF VLHKMLLKPQ QRVTLCDFHT AFFGFLFQGA FAGPRDDYKT KYLKILQQKD
CSNVCDYKAG TCALSDENQR CIDMCSFGPC LNGGTCISHS SGYRCSCAEH YSGRNCETYT
LIVGGKCPEG WWGLAACGPC SCDIEKGYGS NCDMATGACG CKDSSYMDPG SGRCLPCDCN
FPTGALNSSC DRSTGQCYCR GDVIGRRCDK CQDKRAQISH IEGHCESKFN FAKIMQWRL
//