ID A0A0V0VIQ0_9BILA Unreviewed; 1672 AA.
AC A0A0V0VIQ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Neurexin-1a {ECO:0000313|EMBL:KRX63249.1};
GN Name=nrxn1a {ECO:0000313|EMBL:KRX63249.1};
GN ORFNames=T09_6056 {ECO:0000313|EMBL:KRX63249.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX63249.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX63249.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX63249.1};
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: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:KRX63249.1}.
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DR EMBL; JYDN01000033; KRX63249.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00110; LamG; 6.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR15036:SF85; SP2353, ISOFORM A; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1575..1595
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..236
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 232..271
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 276..468
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 476..657
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 660..697
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 700..879
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 901..1081
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1488..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 261..270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1054..1081
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1672 AA; 187590 MW; A224B4317D538F29 CRC64;
MVKQRQRRLY KSCVGVSAFI LLALFGFGAG LVSAITLEGS GSSYARFPRW HQAFENVLSV
ELRTKKPNAL LIYIDDSGLG NFYEISIFEG KIRLQFRLGA RQLKNNATAT QLALNGTTAK
LLQIEEVQVD DGQWHRVVLY HFWETVKLQV DQSVVFSKVL DQQDFVFADY EQSSDVYVGG
LPVAMQASSL SFPFAKALPR FEGSVRNLIY RTVPHGITAP SILQADGIRE SDNDYCTTTT
TSYCSGHGIC YSSDTGPMCN CNLGRYGDTC LSEKKTLEVM LFAGQLFGFD RWSIKNGILS
RSEQVRLQFK TRRQSGLLFL YGNDMEFVRI ALQNGAVSAV SKLQQTVQDA RVVPFKSSFS
DQKLGFGDGQ WHSLTFSRKL NQVKLSVDDV FSSVRDVVEQ SMFYTNFVYV GGMMQSLSNE
TNSLWTNFSG CLRNVHFIAD QRRIDLLEEL NKQSGLVQTV VGNVTRECRQ SFSVEAVTFV
NGHSSLALTN RWTGGNDGQL VAFKFRTNEP YGLLLHCGPA EPHLSDLLAV EIFAGHLYFV
IDLGSGTSRL QASGRLVADG HWHSVNMTRR WRSGQIYVDS WRVDFSTPGK EKMLDTADVV
QFGYSVAEAR NLPPSVWTAT LGRGFVGCLK DVTLDGVSLD LIGLLPHQRQ RDVVVGCYDM
LPQCTEVSCK NGGRCIEGWN RYYCDCSAVF YSGDRCEQEM FVANLESNSQ IVVNFLNPLR
TQVEDVRLKF RSKKVNGLLM LAVDLRRKIC FGLQLVNRRL EFFLSSSTFF QNVHWDVKLR
ENYWHSVALF RTGQRLELVL DGDRLAEKEI LSFVQPFQLR YDRLYVGSAE VDALADQREK
MFYNENDHHF HGEMADFQFN GLQVLTLAWH GQIGHSGGSG LWAVGDVRST NVLYSAERDF
VVSFQADSFA KVSLEKPTTV TLDKLEVSFT FRTTEKNGVL LYRQGDSRNF LLLELFNGRL
ICRFNSTDYK HALQSNHPLP LNDHNWHHVV FYDSAQHTGE IRLVVDNYTS NWSSDSVRPM
PVRYNASLVI GYPGVEVADR LVDVLPSGRG FQGCMVNLKI DGSPVRLLQD SEMQANLRRG
CTKMCPRELC IGKDGCPLEK VPADCDCLLT EISDLYCLNQ SVAYRFGPRP GTVLFRLDEN
SHVGPVPDRV LMGIVTYQAD AVVMQMVTLP DSRQTFELLI ENGYFAVKFR DQYGETVLSE
KSIQLNDGQY HFVQFNRSRL DLTLQIDQQE RVVTKMKGMY VCVWVGGWMG GEHDKIANLH
STLKICPSSS TGQASTTTAT WMKHTDRWIA LGGRFDGQVQ TKRRQFRRGS SLPFNDAFYG
ILSSVLVNDY RLLELASSGD ERVILVGDVR RHHYFNYNES QLNHLEHQQL ETTIPNEETT
TTAATVREDI FDSINDDVDD LEKITSENEE ALDNLQTLMA TDPVQWSSAA AAAAAAAAAS
ATATTTTTTT SMDELLLSGE GDGQQLASCS QLLDDEDCSA EQNELITPVF RFDEPDETEP
SSQSSSGSST SQRQQQQTVT EPNYQKTTID VSGSANSTIE SATFKSVTGR ISTEVATTVK
PNDTLNNKGF PRTSVIAGVS VGLVVVLTLI LFYVFKCRQE PQTAIVADYT SINNNDHNTD
DKSNNISFDK NKHQCNNNNK LNECFAQSMA VMIPRYTSFF PSQSKSVKEW YV
//
