GenomeNet

Database: UniProt
Entry: Q9BZ76
LinkDB: Q9BZ76
Original site: Q9BZ76 
ID   CNTP3_HUMAN             Reviewed;        1288 AA.
AC   Q9BZ76; B1AMA0; Q9C0E9;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 3.
DT   13-FEB-2019, entry version 167.
DE   RecName: Full=Contactin-associated protein-like 3;
DE   AltName: Full=Cell recognition molecule Caspr3;
DE   Flags: Precursor;
GN   Name=CNTNAP3; Synonyms=CASPR3, KIAA1714;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12093160; DOI=10.1006/mcne.2002.1110;
RA   Spiegel I., Salomon D., Erne B., Schaeren-Wiemers N., Peles E.;
RT   "Caspr3 and Caspr4, two novel members of the Caspr family are
RT   expressed in the nervous system and interact with PDZ domains.";
RL   Mol. Cell. Neurosci. 20:283-297(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP   HIS-845.
RC   TISSUE=Brain;
RX   PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA   Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIX.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 7:347-355(2000).
RN   [3]
RP   SEQUENCE REVISION.
RA   Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305};
CC       Single-pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BZ76-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BZ76-2; Sequence=VSP_003535, VSP_003536;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB21805.2; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF333769; AAG52889.2; -; mRNA.
DR   EMBL; AB051501; BAB21805.2; ALT_INIT; mRNA.
DR   EMBL; AL162501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS6616.1; -. [Q9BZ76-1]
DR   RefSeq; NP_387504.2; NM_033655.3. [Q9BZ76-1]
DR   UniGene; Hs.128474; -.
DR   UniGene; Hs.521495; -.
DR   UniGene; Hs.604441; -.
DR   ProteinModelPortal; Q9BZ76; -.
DR   SMR; Q9BZ76; -.
DR   BioGrid; 123011; 54.
DR   STRING; 9606.ENSP00000297668; -.
DR   iPTMnet; Q9BZ76; -.
DR   PhosphoSitePlus; Q9BZ76; -.
DR   BioMuta; CNTNAP3; -.
DR   DMDM; 209572752; -.
DR   EPD; Q9BZ76; -.
DR   jPOST; Q9BZ76; -.
DR   MaxQB; Q9BZ76; -.
DR   PaxDb; Q9BZ76; -.
DR   PeptideAtlas; Q9BZ76; -.
DR   PRIDE; Q9BZ76; -.
DR   ProteomicsDB; 79776; -.
DR   ProteomicsDB; 79777; -. [Q9BZ76-2]
DR   Ensembl; ENST00000297668; ENSP00000297668; ENSG00000106714. [Q9BZ76-1]
DR   GeneID; 79937; -.
DR   KEGG; hsa:79937; -.
DR   UCSC; uc004abi.4; human. [Q9BZ76-1]
DR   CTD; 79937; -.
DR   EuPathDB; HostDB:ENSG00000106714.17; -.
DR   GeneCards; CNTNAP3; -.
DR   H-InvDB; HIX0008061; -.
DR   HGNC; HGNC:13834; CNTNAP3.
DR   HPA; HPA047731; -.
DR   MIM; 610517; gene.
DR   neXtProt; NX_Q9BZ76; -.
DR   OpenTargets; ENSG00000106714; -.
DR   PharmGKB; PA134963289; -.
DR   eggNOG; KOG3516; Eukaryota.
DR   eggNOG; ENOG410XPHG; LUCA.
DR   GeneTree; ENSGT00940000160228; -.
DR   HOGENOM; HOG000230964; -.
DR   HOVERGEN; HBG057718; -.
DR   InParanoid; Q9BZ76; -.
DR   OMA; DHCQQEL; -.
DR   OrthoDB; 338397at2759; -.
DR   PhylomeDB; Q9BZ76; -.
DR   TreeFam; TF321823; -.
DR   GenomeRNAi; 79937; -.
DR   PRO; PR:Q9BZ76; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000106714; Expressed in 90 organ(s), highest expression level in lower esophagus.
DR   ExpressionAtlas; Q9BZ76; baseline and differential.
DR   Genevisible; Q9BZ76; HS.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0008037; P:cell recognition; NAS:UniProtKB.
DR   CDD; cd00057; FA58C; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   InterPro; IPR028873; CASPR3.
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; PTHR43925:SF6; PTHR43925:SF6; 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; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 4.
DR   SUPFAM; SSF56496; SSF56496; 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   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Polymorphism;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26   1288       Contactin-associated protein-like 3.
FT                                /FTId=PRO_0000019509.
FT   TOPO_DOM     26   1245       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1246   1266       Helical. {ECO:0000255}.
FT   TOPO_DOM   1267   1288       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       31    177       F5/8 type C. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN      183    364       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      370    545       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      551    583       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      584    792       Fibrinogen C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   DOMAIN      793    958       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      962    996       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1015   1203       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   COMPBIAS     42     48       Poly-Ser.
FT   CARBOHYD    285    285       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    359    359       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    441    441       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    497    497       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    623    623       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    706    706       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1023   1023       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1073   1073       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1120   1120       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     31    177       {ECO:0000250}.
FT   DISULFID    332    364       {ECO:0000250}.
FT   DISULFID    513    545       {ECO:0000250}.
FT   DISULFID    551    562       {ECO:0000250}.
FT   DISULFID    556    571       {ECO:0000250}.
FT   DISULFID    573    583       {ECO:0000250}.
FT   DISULFID    931    958       {ECO:0000250}.
FT   DISULFID    962    975       {ECO:0000250}.
FT   DISULFID    969    984       {ECO:0000250}.
FT   DISULFID    986    996       {ECO:0000250}.
FT   DISULFID   1167   1203       {ECO:0000250}.
FT   VAR_SEQ    1120   1127       NQSTKKQV -> IPQMQKSN (in isoform 2).
FT                                {ECO:0000303|PubMed:11214970}.
FT                                /FTId=VSP_003535.
FT   VAR_SEQ    1128   1288       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11214970}.
FT                                /FTId=VSP_003536.
FT   VARIANT     628    628       A -> S (in dbSNP:rs1758272).
FT                                /FTId=VAR_046710.
FT   VARIANT     845    845       R -> H (in dbSNP:rs7852039).
FT                                {ECO:0000269|PubMed:11214970}.
FT                                /FTId=VAR_046711.
FT   CONFLICT     21     21       S -> R (in Ref. 1; AAG52889).
FT                                {ECO:0000305}.
FT   CONFLICT     33     33       A -> S (in Ref. 1; AAG52889).
FT                                {ECO:0000305}.
FT   CONFLICT     89     89       M -> I (in Ref. 1; AAG52889).
FT                                {ECO:0000305}.
FT   CONFLICT    711    711       S -> Y (in Ref. 1; AAG52889 and 2;
FT                                BAB21805). {ECO:0000305}.
FT   CONFLICT    714    714       G -> V (in Ref. 2; BAB21805).
FT                                {ECO:0000305}.
FT   CONFLICT    769    771       AGR -> TGQ (in Ref. 1; AAG52889).
FT                                {ECO:0000305}.
FT   CONFLICT    777    777       A -> D (in Ref. 1; AAG52889).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1288 AA;  140690 MW;  F41F1CE8A83D417E CRC64;
     MASVAWAVLK VLLLLPTQTW SPVGAGNPPD CDAPLASALP RSSFSSSSEL SSSHGPGFSR
     LNRRDGAGGW TPLVSNKYQW LQIDLGERME VTAVATQGGY GSSDWVTSYL LMFSDGGRNW
     KQYRREESIW GFPGNTNADS VVHYRLQPPF EARFLRFLPL AWNPRGRIGM RIEVYGCAYK
     SEVVYFDGQS ALLYRLDKKP LKPIRDVISL KFKAMQSNGI LLHREGQHGN HITLELIKGK
     LVFFLNSGNA KLPSTIAPVT LTLGSLLDDQ HWHSVLIELL DTQVNFTVDK HTHHFQAKGD
     SSYLDLNFEI SFGGIPTPGR SRAFRRKSFH GCLENLYYNG VDVTELAKKH KPQILMMGNV
     SFSCPQPQTV PVTFLSSRSY LALPGNSGED KVSVTFQFRT WNRAGHLLFG ELRRGSGSFV
     LFLKDGKLKL SLFQPGQSPR NVTAGAGLND GQWHSVSFSA KWSHMNVVVD DDTAVQPLVA
     VLIDSGDTYY FGGCLDNSSG SGCKSPLGGF QGCLRLITIG DKAVDPILVQ QGALGSFRDL
     QIDSCGITDR CLPSYCEHGG ECSQSWDTFS CDCLGTGYTG ETCHSSLYEQ SCEAHKHRGN
     PSGLYYIDAD GSGPLGPFLV YCNMTADAAW TVVQHGGPDA VTLRGAPSGH PRSAVSFAYA
     AGAGQLRSAV NLAERCEQRL ALRCGTARRP DSRDGTPLSW WVGRTNETHT SWGGSLPDAQ
     KCTCGLEGNC IDSQYYCNCD AGRNEWTSDT IVLSQKEHLP VTQIVMTDAG RPHSEAAYTL
     GPLLCRGDQS FWNSASFNTE TSYLHFPAFH GELTADVCFF FKTTVSSGVF MENLGITDFI
     RIELRAPTEV TFSFDVGNGP CEVTVQSPTP FNDNQWHHVR AERNVKGASL QVDQLPQKMQ
     PAPADGHVRL QLNSQLFIGG TATRQRGFLG CIRSLQLNGV ALDLEERATV TPGVEPGCAG
     HCSTYGHLCR NGGRCREKRR GVTCDCAFSA YDGPFCSNEI SAYFATGSSM TYHFQEHYTL
     SENSSSLVSS LHRDVTLTRE MITLSFRTTR TPSLLLYVSS FYEEYLSVIL ANNGSLQIRY
     KLDRHQNPDA FTFDFKNMAD GQLHQVKINR EEAVVMVEVN QSTKKQVILS SGTEFNAVKS
     LILGKVLEAA GADPDTRRAA TSGFTGCLSA VRFGRAAPLK AALRPSGPSR VTVRGHVAPM
     ARCAAGAASG SPARELAPRL AGGAGRSGPA DEGEPLVNAD RRDSAVIGGV IAVVIFILLC
     ITAIAIRIYQ QRKLRKENES KVSKKEEC
//
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