ID W5LQ93_ASTMX Unreviewed; 1256 AA.
AC W5LQ93;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Contactin associated protein 2 {ECO:0000313|Ensembl:ENSAMXP00000022190.2};
GN Name=CNTNAP2 {ECO:0000313|Ensembl:ENSAMXP00000022190.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000022190.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000022190.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, paranodal septate junction
CC {ECO:0000256|ARBA:ARBA00004403}.
CC -!- SIMILARITY: Belongs to the neurexin family.
CC {ECO:0000256|ARBA:ARBA00010241}.
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 AlphaFoldDB; W5LQ93; -.
DR STRING; 7994.ENSAMXP00000022190; -.
DR Ensembl; ENSAMXT00000022190.2; ENSAMXP00000022190.2; ENSAMXG00000021544.2.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000154516; -.
DR HOGENOM; CLU_003504_2_1_1; -.
DR InParanoid; W5LQ93; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000021544; Expressed in brain and 5 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.1000; -; 1.
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; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF33; CONTACTIN-ASSOCIATED PROTEIN-LIKE 2; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00294; 4.1m; 2.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00122};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1187..1208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..132
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 86..306
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 311..485
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 487..524
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 523..573
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 732..896
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 897..935
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 958..1146
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 869..896
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1256 AA; 139696 MW; 207450FF194AB11C CRC64;
SSSVFTSGYA PGYAKLNRRG GAGGWSPLDS DHYQWLQVDL GSRKQVTAIA TQGRYSSSDW
TTRYRLLYSD TGRNWKPYHQ DGNIWAFTGN SNTESVVRHD LQHAIVAQYL RIIPLDWSEE
GRIGLRLEIY GCPYWADVIN FDGQGVISYR FKMKKMKILK DVIALKFKTQ GDYITLELRR
GRLLLQINLG SNQYGSILGH TSVTSGSLLD DHHWHSVVIE RYRRNVNFTL DQHTQHFRTN
GEFDHLDLDY ELSFGGMPYS GKPISGGRRN FKGCMESINY NGENITDLAR RKKLDTSSFR
NLTFSCVDTH TFPVFFNATS FLQLSGRREH NMISVGFQFR TWNPNGLFLF SSLADGMLEI
SLNDGKVTAH INVTQQKNSR VDIASGSGLN DGEWHDVRFL AKENFAMLTV DGDEASAVRT
NTPIQITTGG TYHFGGYFLR TQASPSQRSF QGCMQLIQVD DQLADLTAVE QGRLGAFENV
SLDMCAIIDR CMPNHCEHGG RCTQTWNSFS CSCDGTGYTG ATCHTSVYEQ SCEAYKHVGR
SSDLYWIDPD GSGPLGPFKV ICNMTEDKVW TTVANNLPAQ TSVTGSSRER RTVLQLNYSA
TMEQISAITS SAEHCEQHVA YNCRMSRLLN TPDGTPYTWW VGRGNEKHFY WGGSAPGIQK
CSCGIERNCT DPKYHCNCDA DQKQWQEDSG LLVYKDHLPV SQVAVGDTNR PGSEAKLTVG
PLRCQGDRSY WNAASFNTPS SYLHFSTFQG ETSADISFYF KTSAPYGVFL ENLGNTDFIR
LELKSPTVVS FSFDVGNGPV ELNVHSPTPL NDDQWHRVSA ERNVKEAILQ LDQQYKEVRP
APAQGHTRLE LYSQLYVGAA GGQRGFLGCI RSLKMNAVTL DLEERAKVTP GVKPGCSGHC
TSFGMYCRNG GKCVEKYNGY SCDCSATAYD GPFCTKDVGG FFEAGTLIRY NLVSDVVAAA
SSVEGKSVGT SLPMETNLTR EDVAFSFSTS STPSILFYIS SKTQDYMAVV LRQNGTLQLR
YNLGGLREPF TIDLDQRNLA NGQPHSVNIT RIERDIYVQL DHYPSVSYTL PEASDTQFNL
VKTLFLGKVF ETGQIDPVLI EKYNTPGFVG CLSRVQFNSI APLKAALSTR ASAPVSHQGK
LVESNCGASP LTIPPMSAAT DPWNQKDPDF PFNEERVIPD GVNRNSAIIG GIIAVVIFTI
LCTLVFLIRY MFRHKGTYHT NEAKGGESSE SADTAIIGTD PNFTETIDES KKEWFI
//
