ID A0A218UKK3_9PASE Unreviewed; 1169 AA.
AC A0A218UKK3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Contactin-associated protein-like 4 {ECO:0000313|EMBL:OWK54265.1};
GN Name=CNTNAP4 {ECO:0000313|EMBL:OWK54265.1};
GN ORFNames=RLOC_00003145 {ECO:0000313|EMBL:OWK54265.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK54265.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK54265.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK54265.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:OWK54265.1}.
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DR EMBL; MUZQ01000244; OWK54265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218UKK3; -.
DR STRING; 299123.ENSLSDP00000017629; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00054; EGF_CA; 2.
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; IPR001791; Laminin_G.
DR PANTHER; PTHR15036:SF40; CONTACTIN-ASSOCIATED PROTEIN-LIKE 4; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR PROSITE; PS50026; EGF_3; 2.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1102..1126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..48
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 54..235
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 241..451
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 453..490
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 489..540
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 654..819
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 820..858
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 870..1063
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1066..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 792..819
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1169 AA; 130106 MW; 136B958946966C25 CRC64;
MAFSGNTNAD SVVYYKLQHS IKARFLRFVP LDWNPNGRIG MRIEVYGCTY RSEVVGFDGK
SCLIYTLNKK LINALKDVIS LKFKTMQSDG ILLHREGQNG DHITMELTKG KLSLLINLGD
TKTHPSNAQI NITLGSLLDD QHWHSVVIEH FNNQVNFTVD KHTHHFHGKG EFSYLDLDYE
LSFGGIPMPG KSGTLSRRNF HGCFENIYYN GVNIIDLARR HKSQIYIVGN MSFSCLEPQV
VPVTFLSSSS FLALQGTSGQ DEVFVSFEFR TWNKEGLLLS SKLHQSSGGF LLYLSDGRVK
INLHKTGRVL SDIATDGLYD VIWFGTVWLD SVQAERDLGV LVDSWLDMSQ QRALVAKKAN
GILACSRNCA GLNNGQWHSV SLAVKRSRIS VRVDNDVTTS AHAFIPLQIY SDVFYFGGCM
RHISIGNKAV DMISIQQNGF GNFSDLLIDL CGITDRCLPN YCEHGGECSQ SWNSFHCNCA
NTGYKGATCH YPIYEQSCEA YKHRGITSGF YNIDSDGSGP LGPFLVYCNM TDATWTIIQH
NSTNLTRVKN ANRENPHTVF FKYSASLDQL QATINLADHC EQELAYYCKK SRLLDKSETK
VLDQLTRTND TGFLSYKDHL PVTEIVITDT DRPNSEAAYK LGPLLCRGDR TFWNSASFNT
EASYLHFPTF HGEFSADVSF FFKTTASSGV FLENLGIQDF IRIELQSPSE VAFSFDVGNG
PSEVVVQSHN SLNDNQWHYV KAERNVKEAS LQIDQLPQRS HSAPPDGHIR LQLNSQLFVG
GTASRQKGFL GCIRSLRLNG MALDLEERAK ITPGVEPGCP GHCSSYGNLC HNGGKCREKY
SGFSCDCTFS AYAGPFCKKE ISAYFWTGTS VTYNFQEYYT LAKNSSSHAS SFYADMTLAR
EAITFAFRTT RTPSLLLYVS SFYKEYLSAI LTRNGSLQIR YKLDSHQDPD VFSISFKSMA
DGQLQHVKIN REEETLFVEV NQNERMKFIL SSGTEFNAIK SLTLGKILEN SDVDEETMKA
NSQGFVGCLS SVQFNHIAPL KAALHHSSSA PVIVKGRFTE SSCGALTGAD STSSETTHSF
ADHSGPIDEG KPLANAIRSD SAIIGGVIAV VIFILLCITA IAIRIYKKKG IYSKNEAKGS
ENEDSAESAL KSELSMQNTA NENQKEYFF
//
