ID A0A3Q2W4Y2_HAPBU Unreviewed; 1293 AA.
AC A0A3Q2W4Y2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Contactin associated protein 2 {ECO:0000313|Ensembl:ENSHBUP00000020478.1};
GN Name=CNTNAP2 {ECO:0000313|Ensembl:ENSHBUP00000020478.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000020478.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000020478.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR Ensembl; ENSHBUT00000030106.1; ENSHBUP00000020478.1; ENSHBUG00000022907.1.
DR GeneTree; ENSGT00940000154516; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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 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; SM00181; EGF; 2.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00122}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1293
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018704629"
FT DOMAIN 33..183
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 189..370
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 375..550
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 552..589
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 588..640
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 797..961
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 962..1000
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1020..1224
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 934..961
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1293 AA; 143114 MW; 74AE90C400287F59 CRC64;
MRRHRPAQGL TLLLPVVLWI FCHASGVHGA LPTTQKCDEA LASPLPHTAF TSSSVFSSGY
APGYAKLNRR GGAGGWSPLD SDHYQWLQVD LGSRKQVSAI ATQGRYSSSD WTTQYRLLYS
DTGRNWKPYH QDGNIWAFSG NSNSESAVRH ELQQGIVARF LRLIPLEWSE EGRIGLRIEV
YGCSYWADII NFDGQGVISY RFKVKKMKII KDVIALRFKT SESEGVILHG EGQQGDYITL
ELRKAKLLLQ INLGSNQYGS ILGHTSVTTG SLLDDNHWHS VVIERYRRNV NFTLDRHTQH
FRTNGEFDHL DLDYELSFGG MPYSGKPVGI GRKNFKGCME SINYNGDNIT DLARRKKLDT
SSFRNLSFTC AETHTFPVFF NATSFLQLPG RANHNTVSVG FQFRTWNPHG LLLFSNLDDG
TLEISLEDGK VAVHINVTKA AKSYRVDLSS GSGLNDGQWH AIRLVAKENF AMLTIDGEEV
SAVRSVSPLS ITTGGTYHLG GYFLQTLFPP TQRSFQGCMQ AVLVDDQPAD LHAVEKGTVG
AFENVSLDMC AIIDRCMPNH CEHGGRCKQT WDSFSCTCDG TGYTGATCHT SIYEPSCEAY
KHLGKSSDAY WIDPDGSGPL GPFKVNCNMT EDKVWTTVMN NLPPKTIVTG SSRNRRTVLQ
VNYSASMDQV TAITTSAEYC EQQIAYSCRM SRLLNTPDGT PYTWWVGRGN EKHFYWGGSG
PGIQKCACGI DRNCTDPKYD CNCDADVKQW REDSGLLVYQ EHLPVSQVVV GDTNRSGSEA
KLTVGPLRCQ GDNNYWNAAS FTTPSSYLHF ATFQGETSAD ISFYFKTSAA YGVFLENLGN
TDFIRLELKS PKVVSFSFDV GNGPVELIVH SATSLNDDQW HRVMAERNVK EAVLQLDQTY
RTSRLAPAQG HTRLELFSQL YVGAAGGQRG FLGCIRALRM NGITLDLEER AKVTPGVKPG
CQGHCNSFGM YCRNGGKCVE RYNGYLCDCT ATAYDGPFCT RDVGGFFEAG TLVKYNFLPE
AIAGASKDTK VLTHQLTPHE VNLTKEEVAF SFSTSSAPAV LMYVSSKTQD YLAVVLRQNG
SLQVRYNLGG LREPFTIDVD QRNLANGQPH SINMSRHDRR ITIQLDHYPA VSYNLPEASD
TQFNLVKTLF LGKVYETGHI DPVIIERYNT PGFIGCLSRV EFNGIAPLKS ALRTAVKSQA
TPTEKQPAAA SPASYQGKLV ESNCGASPLT IPPMSAATDP WHLDKTDAVF PFNEERVIPD
GVNRDSAIIG GTKCHYHIIK LKVLKHGGFF IAN
//
