ID   CNTN5_DANRE             Reviewed;        1056 AA.
AC   Q7ZW34;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Contactin-5;
DE   Flags: Precursor;
GN   Name=cntn5; ORFNames=zgc:55318;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC       system development. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC       family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other members of the family, it lacks a
CC       canonical signal sequence; the existence of the signal sequence is
CC       therefore unsure. {ECO:0000305}.
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DR   EMBL; BC045307; AAH45307.1; -; mRNA.
DR   RefSeq; NP_956098.1; NM_199804.1.
DR   AlphaFoldDB; Q7ZW34; -.
DR   SMR; Q7ZW34; -.
DR   STRING; 7955.ENSDARP00000089410; -.
DR   PaxDb; Q7ZW34; -.
DR   GeneID; 327429; -.
DR   KEGG; dre:327429; -.
DR   CTD; 53942; -.
DR   ZFIN; ZDB-GENE-030131-5640; cntn5.
DR   eggNOG; KOG3513; Eukaryota.
DR   InParanoid; Q7ZW34; -.
DR   OrthoDB; 655902at2759; -.
DR   PhylomeDB; Q7ZW34; -.
DR   PRO; PR:Q7ZW34; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.10; -; 10.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 3.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 6.
DR   SUPFAM; SSF48726; SSF48726; 6.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW   Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..1035
FT                   /note="Contactin-5"
FT                   /id="PRO_0000014723"
FT   PROPEP          1036..1056
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014724"
FT   DOMAIN          57..142
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          154..240
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          258..343
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          348..432
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          438..519
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          527..622
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          629..727
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          732..829
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          834..928
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          933..1023
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1035
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        496
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        772
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        887
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        945
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        958
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        175..227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        280..327
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        369..416
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        459..507
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        549..606
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   1056 AA;  116202 MW;  C6BD5C9A2520347F CRC64;
     MKADSSSSSS MSSRMRLRNS HGVGSSSQDW SPFSRHRYSA LSSQEDYRSE ESEEFGPVFI
     QEPDDAIFSL DSDDKKIIMN CEARGNPVPT YSWLINGTNV DTEADFRYSL IDGNLIIHNA
     SEVIDYGRYQ CRAENSIGIV LSRDALLQFA YLGPFSGKTR GAVSVREGQG VVLMCAPPSH
     SPEIIYSWVF NELPSFVAED SRRFISQETG NLYIPKVQPS DVGSYVCQVK NTVTNARVLS
     PPTPLTLKTD GVMGEYEPKI EAHFPQTVLA AKGVTVRLEC FALGNPVPTI TWRKMSGNIP
     KKARLRKSQA VLEIPNIQLE DSGSYECKAE NTRGGTAFRG HLQVYTLPQW ISMINDTQLD
     SGEQLRWECR ATGKPRPTYR WLRNGEPLST QSRVEMVNGE LTIHRLQQAD SGMYQCIAEN
     KYGAIYSSAE LKILASAPMF NNNPVRLIAT VGKDVSLECR PRASPKPRIS WRKNDRRLQP
     SRRIMLLRNN TLRIINSSRS DEGSYVCRAE NQFGSAELTT VLLVKEPMRV ELSPLRVEVT
     VGESVVLSCK VTHDPSLDVS FLWLLNNQPL NTQQDGGHFE YIQTQSSTAD LMIRSILLKH
     AGKYGCRAQT STDSVLAEAE LLVRGPPGPP GVVIVEEITA STATLSWSHG VDNHSPITTY
     NVQARSPVSL GWQTVKTDPD PVTGSMESAM AVDLNPWVEY EFRVVATNSI GTGDPSPPSR
     AVRTKEAVPS VAPANVRGGN GRRHELVISW EPVSEEYQNG EGFGYIVAFR VNGTRGWKEK
     MVTSADSTTY KYRDETFPPL TPFEVRVGVY NNKGDGPFSE VVTVFSAEGE PREPPSEVQA
     FAVSSSEIKV LWKPPSPGLG RPQGYEVSFW KDVEQEELGK KKRTLGNETN MLLSGLDGNT
     QYLVSVKGFN SAGQGPSSTA VKISTKKNAP SLPPGNLMWI QEGNNVSLSW DPVKARDNES
     EVIGYKVLLR QEGRGHSQVM RTPNSAVVLT LPEGGTYIIE VRAVSEGGEG AASAQVRVLT
     SSGVRAKNGQ LSVQNSPPGL AWTALFLSLM VPSFPL