ID A0A0V1ME29_9BILA Unreviewed; 1600 AA.
AC A0A0V1ME29;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Contactin-associated protein-like 2 {ECO:0000313|EMBL:KRZ70129.1};
GN Name=Cntnap2 {ECO:0000313|EMBL:KRZ70129.1};
GN ORFNames=T10_7759 {ECO:0000313|EMBL:KRZ70129.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ70129.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ70129.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ70129.1};
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:KRZ70129.1}.
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DR EMBL; JYDO01000120; KRZ70129.1; -; Genomic_DNA.
DR STRING; 268474.A0A0V1ME29; -.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR001791; Laminin_G.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR15036:SF85; SP2353, ISOFORM A; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
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:UP000054843};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1600
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006882467"
FT TRANSMEM 1441..1464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 223..261
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 456..494
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 493..548
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 696..871
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 872..911
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 919..1129
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1175..1380
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1568..1600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 231..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 880..897
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1600 AA; 182194 MW; FD3AD7139D449E79 CRC64;
MIKSTTFFFV RLTLIAWMCA RWLQPCTADT AQSNTMINSQ WRTLLSSRSR LVSTKQYFHC
SRADAILNYQ FEITTRSYTG RLGTIYAEQM SSNGTPFRLE LFLQHRKLHL QLVANNHTLA
ALQHALTDFS DGYPHHISAT LHCSTGELGL GVDDELVQTA VVDHHHFNAT TTLDHLKLQM
KFGYDSNALM KHIPAIVGCI RASIFNNESE IESHSSDVQN GCVDHCKTNP CRNVAAHRCI
NLFGNLRCNC LYSGFQGMRC ESQGTVSVVV KKNQHLIYKL PQYENQPSKF VLNFKSNVQS
RQELLKISLL SVSNENRALI SVDIVNQSLV EIFYGQRKPL QCSLPLSEND KRQVHFVEFQ
LIFEYSIQEI HVQTVSGGNR CQFWPNILED SFVLRDVIIG SNQSEGFVGC VKNFYLDFTN
VLWLTKVAGQ QQLISNEQIA FGCGEVPTLW SYKLVNHSAC DTRRCRHHSS CIDDGRNGAR
CSCATMPYAG SLCQFSTLEK SCHHLYRMGN HHSGVYRIDP DGSGPIAPVY VYCTMDDELK
HGWTIVEHNF EESMQIRSVW AKDATYIISY SHFSLNALRY LIVNSHFCRQ HFVYTCNNAP
IYFPTYTWFR SATMYGNFST LIFEKNACFC YANKTCARAG RCNCDGSELN AHADAGYLVN
HQAGLIEMTF IQHRPRKGWA NVALGPLECR GSDLEEAIQF FGAGTIIEES AWKGINLEIW
FKTTNSESTI LFNQEADDGR FFRILLNKGT VVDFQFDFNL RRDQNDGMKT VTLEDLNGSS
YASNEWTRIK VENIDSEIFF VLNRKQAFYK LAEYEQLDRT TFDKPLMIGG RQSISENRFV
GCIGELVIDK RRIPLQTFLT ENSARGLKLG CQNYCAHLNC ANGALCSEDY ANGVARCKCK
NSYAHFGSLC EIDINEQSDV SFQRKDNGFI MYRDLRQNPL VEQIVLSFRT DQESGLLFYA
HDQFYNFIQL HLWESNRLSL TVNSDREVKQ CTAIGKTSKF NNMEWKQVAV VRRGHVIHLY
VEDVSCKIDA TTWMSRNYVT SFIDPYNFQT VIPPRPPVAP NNMSNYTLTY VGGLPSQAFY
TTRKRRQAVY ATKLQNYLGC MRGLRIGSDD VDLKKAGERT TDSPDSSGCR FYSKSSLICY
NGGHFTVDWS TRTLNEQCHC SDTAFSGKNC SHDEGVHFTG HSVLSFRLDK LFASSHGAMG
LFGQTSDLLR FVFITPFKLR DRQAMLLIEK SRPLKGSYFN IMLFNNELAF QIFDDKQLSS
VIYHFYGNYL NDKPHLVLLQ LYNDFKMIIR VDDQEKEVPL LDSTILRRGE LLVGGFRQLS
SSANVTKYRG CISNLLIENN AIVGESIALF ELVKTVGFTD PERRFRLYSI NNEDVHLSPC
GLITEALQPL TTPVSLTMPA WDRLLETRIY ADNIELEDVF TRLTTPSNEN DFAEKSDGES
AGIAVGFIIF ISVVVVLMFA ILLWRKVQRK SYITHEMYED EDDFSELDDE FQNERCYCHQ
AETAEEHGIG GLNATDSSSQ CVNNVSPDEM DKLKDSQDII SPTNLGSYEC SSGDLKYMDE
NVNRLSREYP PAAPLQQNQM ADQEQQHNRR LVAVSPPKLQ
//