ID I3JVI0_ORENI Unreviewed; 1221 AA.
AC I3JVI0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Contactin associated protein-like 5a {ECO:0000313|Ensembl:ENSONIP00000012875.2};
GN Name=CNTNAP5 {ECO:0000313|Ensembl:ENSONIP00000012875.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000012875.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000012875.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in the correct development and proper
CC functioning of the peripheral and central nervous system and be
CC involved in cell adhesion and intercellular communication.
CC {ECO:0000256|ARBA:ARBA00003165}.
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 AlphaFoldDB; I3JVI0; -.
DR Ensembl; ENSONIT00000012885.2; ENSONIP00000012875.2; ENSONIG00000010241.2.
DR GeneTree; ENSGT00940000160532; -.
DR Proteomes; UP000005207; 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; 1.
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 NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR15036:SF46; CONTACTIN-ASSOCIATED PROTEIN-LIKE 5; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1152..1178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..112
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 118..298
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 305..465
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 467..504
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 503..555
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 712..877
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 878..916
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 936..1119
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 850..877
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1221 AA; 136203 MW; E25131248C755B8E CRC64;
GAGGWSPMVT DQEPWLQVDL REQMEVTAVA TQGRYDSWDW VSSYLLLYSD TGRAWKQYRH
EDGVGRFVGN GNSETIVQNK LSHPVRTRFL RFVPLDWNPS GWMGLRVEVY GCSYKSYVAD
FDGRSSLLYR FNQKSMSTVK DVISLRFKSH QAEGVLLHGE GQRGDYITLE LHRGRLDLYL
NLDDSRARFS SHRVPVTVGS LLDDQHWHSV HIERFNKQVN LTVDSYTQRF QTKGEGHSLE
VDYELSFGGI PLPGKPGTFL RKNFNGCMEN LYYNGINVID LAKRRKPQIH SGNVTFSCSQ
PQLVACTFVS SSSSFLSLPS ASPGAGGFSI RFQFRTWNPE GLLLSVQLNP DPQKLRLQIS
NSWLRLTLHI SDGLWHSVSL DARNLQITLT VDNEPSSTIE LWEQVQSRGS FYFGGCPATA
PDCQGFAPAF QGCMQLIFIN SQLMNLSHVQ QGLLGNYNEL QFDTCNIKDR CLPNLCEHGA
RCSQMWSSFS CDCSGTGYAG ATCHNSIYES SCEAYKLSGS SSGFYFIDPD GSGPLGPTQV
YCNMTEKKVW TVLSHNSTAP VTVQTSSLQK PHVMIFNYSA SAEQLRAIVS GSEQCQQEVV
YNCRKSRLFN TKDGSPLSWW LDREGEKRSY WGGFLPGVQQ CSCSLEENCI DMNYFCNCDA
DTDTWANDTG VLSYKDHLPV SQIVIGDTDR MGSQAVYHIG PLRCYGDRSI WNAASFYQES
SYLYFPTLQA ELASDISFYF KTSAPSGVFL ENQGLKDFIR VELSSPSVVT FSFDVGNGPA
VLSVKSHVPL NDRQWHYVRA ERNAKEASVQ VDQLPLRFLE APADGHLRLR LSSQLFVGGT
ASQQRGFLGC IRSLTVNGVS FDLEERAKMT PGVSAGCPGY CTGSSSLCHN RGRCVEKSNG
YICDCSQSAY GGTTCNQEVS VSFDRESSVT YTFQEPFSVM QNRSSQASTS STDSRAREDV
ALSFVTSQRP AMLLTVSTFS QQYIAVILAT NGSVQIWYHL QTDKKPDVFT PTPSNLADGR
LHRIRIHRVG KNLYINQDIH RKYTLSSDAE LILIRSLTLG KVPSEKHFSL LGLIQGASKG
FIGCLSSVQF NHVAPLKVAL TNRGSSLVTI RGPLVQSNCG ALAESHTLQG KTSTSMTLMI
YLFRLTNTRK DLAVIAGVVT AVVFITVCAL AVVIRLVYQQ RRAQRSSGSI KEEHRHSMYT
DYRTELHLHN PVRDSVKEYY I
//
