ID A0A2K5WT80_MACFA Unreviewed; 1330 AA.
AC A0A2K5WT80;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Contactin associated protein 2 {ECO:0000313|Ensembl:ENSMFAP00000040405.2};
GN Name=CNTNAP2 {ECO:0000313|Ensembl:ENSMFAP00000040405.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000040405.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000040405.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000040405.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR STRING; 9541.ENSMFAP00000040405; -.
DR Ensembl; ENSMFAT00000014673.2; ENSMFAP00000040405.2; ENSMFAG00000046348.2.
DR VEuPathDB; HostDB:ENSMFAG00000046348; -.
DR GeneTree; ENSGT00940000154516; -.
DR OrthoDB; 4255614at2759; -.
DR Proteomes; UP000233100; Chromosome 3.
DR Bgee; ENSMFAG00000046348; Expressed in frontal cortex and 5 other cell types or tissues.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0021761; P:limbic system development; IEA:Ensembl.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0071109; P:superior temporal gyrus development; IEA:Ensembl.
DR GO; GO:0021794; P:thalamus development; IEA:Ensembl.
DR GO; GO:0042297; P:vocal learning; IEA:Ensembl.
DR GO; GO:0071625; P:vocalization behavior; IEA:Ensembl.
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; 2.
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 InterPro; IPR003585; Neurexin-like.
DR NCBIfam; NF040941; GGGWT_bact; 1.
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; 1.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00122}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1330
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030052375"
FT TRANSMEM 1261..1282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..180
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 186..367
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 372..551
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 553..590
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 589..641
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 798..962
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 963..1001
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1022..1213
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 935..962
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1330 AA; 148208 MW; 029B8271F5C946B9 CRC64;
MLAAPRAGCA VLLLWIVSSC LCRAWTAPST SQKCDEPLVS GLPHVAFSSS SSMTGSYSPG
YAKINKRGGA GGWSPSDSDH YQWLQVDFGN RKQISAIATQ GRYSSSDWVT QYRMLYSDTG
RNWKPYHQDG NIWAFPGNVN SDGVVRHELQ HPVIARYVRI VPLDWNGEGR IGLRIEVYGC
SYWADVINFD GHVVLPYRFR NKKMKTLKDV IALKFKTSES EGVILHGEGQ QGDYITLELK
KAKLVLSLNL GSNQLGPIYG HTSVMTGSLL DDHHWHSVVI ERQGRSINLT LDRSMQHFRT
NGEFDYLDLD YEITFGGIPF SGKPSSSGRK NFKGCMESIN YNGINITDLA RRKKLEPSNV
GNLSFSCVEP YTVPVFFNAT SYLEVPGRLN QDLFSVSFQF RTWNPNGLLV FSHFADNLGN
VEIDLTESKV GVHINITQTK MSQIDISSGS GLNDGQWHEV RFLAKENFAI LTIDGDEASA
VRTNSPLQVK TGEKYFFGGF LNQMNNSSHS VLQPSFQGCM QLIQVDDQLV NLYEVAQRKP
GSFANVSIDM CAIIDRCVPN HCEHGGKCSQ TWDSFRCTCD ETGYSGATCH NSIYEPSCEA
YKHLGQTSNY YWIDPDGSGP LGPLKVYCNM TEDKVWTIVS HDLQMQTNVV AYNPEKYSVT
QLVYSASMDQ ISAITDSAEY CEQYVSYFCK MSRLLNTPDG SPYTWWVGKA NEKHYYWGGS
GPGIQKCACG IERNCTDPKY YCNCDADYKQ WRKDAGFLSY KDHLPVSQVV VGDTDRQGSE
AKLSVGPLRC QGDRNYWNAA SFPNPSSYLH FSTFQGETSA DISFYFKTLT PWGVFLENMG
KEDFIKLELK SATEVSFSFD VGNGPVEIIV RSPTPLNDDQ WHRVTAERNV KQASLQVDRL
PQQIRKAPTE GHTRLELYSQ LFVGGAGGQQ GFLGCIRSLR MNGVTLDLEE RAKVTSGFIS
GCSGHCTSYG TNCENGGKCL ERYHGYSCDC SNTAYDGTFC NKDVGAFFEE GMWLRYNFQA
PAINARDSGS RVENSPDQQN SHPDLAQEEI RFSFSTTKAP CILLYISSFT TDFLAVLVKP
TGSLQIRYNL GGTREPYNID VDHRNMANGQ PHSVNITRHE KTIILKLDHY PSMSYHLPSS
SDTLFNSPKS LFLGKVIETG KIDQEIHKYN TPGFTGCLSR VQFNQIAPLK AALRQTNASA
HVHIQGELVE SNCGASPLTL SPMSSATDPW HLDHLDSASA DFPYNPGQGQ AIRNGVNRNS
AIIGGVIAVV IFTILCTLVF LIRYMFRHKG TYHTNEAKGA ESAESADAAI MNNDPNFTET
IDESKKEWLI
//
