CNT3B_HUMAN
ID CNT3B_HUMAN Reviewed; 1288 AA.
AC Q96NU0; A0A087WUH3; B1B0V7; B1B0V8; B1B0V9; B1B0W0; B1B0X8; B1B162; Q4VXF0;
AC Q9H7W3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Contactin-associated protein-like 3B;
DE AltName: Full=Cell recognition molecule Caspr3b;
DE Flags: Precursor;
GN Name=CNTNAP3B; Synonyms=CASPR3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Glial tumor, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP GENE DUPLICATION.
RX PubMed=15820314; DOI=10.1016/j.ygeno.2005.01.002;
RA Boyadjiev S.A., South S.T., Radford C.L., Patel A., Zhang G., Hur D.J.,
RA Thomas G.H., Gearhart J.P., Stetten G.;
RT "A reciprocal translocation 46,XY,t(8;9)(p11.2;q13) in a bladder exstrophy
RT patient disrupts CNTNAP3 and presents evidence of a pericentromeric
RT duplication on chromosome 9.";
RL Genomics 85:622-629(2005).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96NU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96NU0-2; Sequence=VSP_034153, VSP_034154, VSP_034155,
CC VSP_034156;
CC -!- MISCELLANEOUS: The gene encoding CNTNAP3B is the result of a
CC pericentromeric duplication of the genomic region encoding CNTNAP3 on
CC chromosome 9.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI16324.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI16325.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI95321.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK054645; BAB70782.1; -; mRNA.
DR EMBL; AL953854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX664735; CAI16324.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX649569; CAI16324.1; JOINED; Genomic_DNA.
DR EMBL; CR788268; CAI16324.1; JOINED; Genomic_DNA.
DR EMBL; BX664735; CAI16325.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX649569; CAI16325.1; JOINED; Genomic_DNA.
DR EMBL; CR788268; CAI16325.1; JOINED; Genomic_DNA.
DR EMBL; BX664735; CAI16326.1; -; Genomic_DNA.
DR EMBL; BX649569; CAI16326.1; JOINED; Genomic_DNA.
DR EMBL; CR788268; CAI16326.1; JOINED; Genomic_DNA.
DR EMBL; BX664735; CAI95321.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX649569; CAI95321.1; JOINED; Genomic_DNA.
DR EMBL; CR788268; CAI95321.1; JOINED; Genomic_DNA.
DR CCDS; CCDS75836.1; -. [Q96NU0-1]
DR RefSeq; NP_001188309.2; NM_001201380.2. [Q96NU0-1]
DR AlphaFoldDB; Q96NU0; -.
DR SMR; Q96NU0; -.
DR IntAct; Q96NU0; 15.
DR STRING; 9606.ENSP00000478671; -.
DR GlyGen; Q96NU0; 3 sites, 2 O-linked glycans (1 site).
DR iPTMnet; Q96NU0; -.
DR PhosphoSitePlus; Q96NU0; -.
DR BioMuta; CNTNAP3B; -.
DR DMDM; 190358858; -.
DR EPD; Q96NU0; -.
DR MassIVE; Q96NU0; -.
DR MaxQB; Q96NU0; -.
DR PaxDb; Q96NU0; -.
DR PeptideAtlas; Q96NU0; -.
DR PRIDE; Q96NU0; -.
DR ProteomicsDB; 77558; -. [Q96NU0-1]
DR ProteomicsDB; 77559; -. [Q96NU0-2]
DR TopDownProteomics; Q96NU0-2; -. [Q96NU0-2]
DR Antibodypedia; 58807; 22 antibodies from 4 providers.
DR DNASU; 728577; -.
DR Ensembl; ENST00000377561.7; ENSP00000478671.2; ENSG00000154529.15. [Q96NU0-1]
DR GeneID; 728577; -.
DR KEGG; hsa:728577; -.
DR MANE-Select; ENST00000377561.7; ENSP00000478671.2; NM_001201380.3; NP_001188309.2.
DR UCSC; uc064thx.1; human. [Q96NU0-1]
DR CTD; 728577; -.
DR GeneCards; CNTNAP3B; -.
DR HGNC; HGNC:32035; CNTNAP3B.
DR HPA; ENSG00000154529; Low tissue specificity.
DR neXtProt; NX_Q96NU0; -.
DR OpenTargets; ENSG00000154529; -.
DR VEuPathDB; HostDB:ENSG00000154529; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000160228; -.
DR HOGENOM; CLU_066153_0_0_1; -.
DR InParanoid; Q96NU0; -.
DR OMA; DENTWMV; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q96NU0; -.
DR TreeFam; TF321823; -.
DR PathwayCommons; Q96NU0; -.
DR SignaLink; Q96NU0; -.
DR BioGRID-ORCS; 728577; 72 hits in 989 CRISPR screens.
DR ChiTaRS; CNTNAP3B; human.
DR GenomeRNAi; 728577; -.
DR Pharos; Q96NU0; Tdark.
DR PRO; PR:Q96NU0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96NU0; protein.
DR Bgee; ENSG00000154529; Expressed in mucosa of stomach and 99 other tissues.
DR ExpressionAtlas; Q96NU0; baseline and differential.
DR Genevisible; Q96NU0; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
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; PTHR15036:SF36; PTHR15036:SF36; 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; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1288
FT /note="Contactin-associated protein-like 3B"
FT /id="PRO_0000339353"
FT TOPO_DOM 26..1245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1246..1266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1267..1288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..177
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 183..364
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 370..545
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 547..584
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 585..792
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DOMAIN 793..958
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 959..997
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1016..1203
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 23..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..177
FT /evidence="ECO:0000250"
FT DISULFID 332..364
FT /evidence="ECO:0000250"
FT DISULFID 513..545
FT /evidence="ECO:0000250"
FT DISULFID 551..562
FT /evidence="ECO:0000250"
FT DISULFID 556..571
FT /evidence="ECO:0000250"
FT DISULFID 573..583
FT /evidence="ECO:0000250"
FT DISULFID 931..958
FT /evidence="ECO:0000250"
FT DISULFID 962..975
FT /evidence="ECO:0000250"
FT DISULFID 969..984
FT /evidence="ECO:0000250"
FT DISULFID 986..996
FT /evidence="ECO:0000250"
FT DISULFID 1167..1203
FT /evidence="ECO:0000250"
FT VAR_SEQ 493..586
FT /note="GCLGNSSGSGCKSPLGGFQGCLRLITIGDKAVDPILVQQGALGSFRDLQIDS
FT CGITDRCLPSYCEHGGECSQSWDTFSCDCLGTGYTGETCHSS -> A (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034153"
FT VAR_SEQ 626
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034154"
FT VAR_SEQ 694..698
FT /note="DGTPL -> GLVTQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034155"
FT VAR_SEQ 699..1288
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034156"
FT CONFLICT 33
FT /note="S -> A (in Ref. 1; BAB70782)"
FT /evidence="ECO:0000305"
FT CONFLICT 316..317
FT /note="LS -> PT (in Ref. 1; BAB70782)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="R -> S (in Ref. 1; BAB70782)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="V -> I (in Ref. 1; BAB70782)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="P -> L (in Ref. 1; BAB70782)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="L -> R (in Ref. 1; BAB70782)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="H -> Y (in Ref. 2; CAI16324/CAI16326)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="T -> S (in Ref. 2; CAI16324/CAI16326)"
FT /evidence="ECO:0000305"
FT CONFLICT 1175
FT /note="C -> R (in Ref. 2; CAI16326)"
FT /evidence="ECO:0000305"
FT CONFLICT 1247
FT /note="I -> M (in Ref. 2; CAI16326)"
FT /evidence="ECO:0000305"
FT CONFLICT 1254
FT /note="E -> V (in Ref. 2; CAI16326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1288 AA; 140415 MW; 11852910E1338C58 CRC64;
MASVAWAVLK VLLLLPTQTW SPVGAGNPPD CDSPLASALP RSSFSSSSEL SSSHGPGFSR
LNRRDGAGGW TPLVSNKYQW LQIDLGERME VTAVATQGGY GSSDWVTSYL LMFSDGGRNW
KQYRREESIW GFPGNTNADS VVHYRLQPPF EARFLRFLPL AWNPRGRIGM RIEVYGCAYK
SEVVYFDGQS ALLYTLDKKP LKPIRDVISL KFKAMQSNGI LLHREGQHGN HITLELIKGK
LVFFLNSGNA KLPSTIAPVT LTLGSLLDDQ HWHSVLIELL DTQVNFTVDK HTHHFQAKGD
SSNLDLNFEI SFGGILSPGR SRAFTRKSFH GCLENLYYNG VDVTELAKKH KPQILMMGNV
SFSCPQPQTV PVTFLSSRSY LALPGNSGED KVSVTFQFRT WNRAGHLLFG ELQRGSGSFV
LFLKDGKLKL SLFQAGQSPR NVTAGAGLND GQWHSVSFSA KWSHMNVVVD DDTAVQPLVA
VLIDSGDTYY FGGCLGNSSG SGCKSPLGGF QGCLRLITIG DKAVDPILVQ QGALGSFRDL
QIDSCGITDR CLPSYCEHGG ECSQSWDTFS CDCLGTGYTG ETCHSSLYEQ SCEAHKHRGN
PSGLYYIDAD GSGPLGPFLV YCNMTADSAW TVVRHGGPDA VTLRGAPSGH PLSAVSFAYA
AGAGQLRAAV NLAERCEQRL ALRCGTARRP DSRDGTPLSW WVGRTNETHT SWGGSLPDAQ
KCTCGLEGNC IDSQYYCNCD AGQNEWTSDT IVLSQKEHLP VTQIVMTDTG QPHSEADYTL
GPLLCRGDKS 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 QSAKKQVILS SGTEFNAVKS
LILGKVLEAA GADPDTRRAA TSGFTGCLSA VRFGCAAPLK AALRPSGPSR VTVRGHVAPM
ARCAAGAASG SPARELAPRL AGGAGRSGPV DEGEPLVNAD RRDSAVIGGV IAVEIFILLC
ITAIAIRIYQ QRKLRKENES KVSKKEEC
