CNTP4_HUMAN
ID CNTP4_HUMAN Reviewed; 1308 AA.
AC Q9C0A0; E9PFZ6; Q86YZ7;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Contactin-associated protein-like 4;
DE AltName: Full=Cell recognition molecule Caspr4;
DE Flags: Precursor;
GN Name=CNTNAP4; Synonyms=CASPR4, KIAA1763;
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 [MRNA] (ISOFORM 2), AND VARIANTS ARG-786 AND GLU-1155.
RC TISSUE=Brain;
RA Hirano K., Sano M., Murahashi Y., Miyauchi A., Gonoi T., Okabayashi K.;
RT "ProX human full-length cDNA cloning project.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-786
RP AND GLU-1155.
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. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Yamakawa H., Kikuno R.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP INTERACTION WITH TIAM1.
RX PubMed=20361982; DOI=10.1016/j.jmb.2010.03.047;
RA Shepherd T.R., Klaus S.M., Liu X., Ramaswamy S., DeMali K.A., Fuentes E.J.;
RT "The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix
RT adhesion.";
RL J. Mol. Biol. 398:730-746(2010).
RN [6]
RP INTERACTION WITH TIAM1.
RX PubMed=23395182; DOI=10.1016/j.str.2013.01.004;
RA Liu X., Shepherd T.R., Murray A.M., Xu Z., Fuentes E.J.;
RT "The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a
RT ligand conformation that modulates protein dynamics.";
RL Structure 21:342-354(2013).
CC -!- FUNCTION: Presynaptic protein involved in both dopaminergic synaptic
CC transmission and GABAergic system, thereby participating in the
CC structural maturation of inhibitory interneuron synapses. Involved in
CC the dopaminergic synaptic transmission by attenuating dopamine release
CC through a presynaptic mechanism. Also participates in the GABAergic
CC system (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TIAM1. {ECO:0000269|PubMed:20361982,
CC ECO:0000269|PubMed:23395182}.
CC -!- INTERACTION:
CC Q9C0A0-1; Q13009: TIAM1; NbExp=2; IntAct=EBI-16035743, EBI-1050007;
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q99P47}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q99P47}. Note=Specifically present within the
CC presynaptic compartment of synapses. {ECO:0000250|UniProtKB:Q99P47}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0A0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0A0-2; Sequence=VSP_044464, VSP_044465;
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21854.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB100093; BAC55271.1; -; mRNA.
DR EMBL; AB051550; BAB21854.2; ALT_INIT; mRNA.
DR EMBL; AC010528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS10924.2; -. [Q9C0A0-2]
DR CCDS; CCDS73915.1; -. [Q9C0A0-1]
DR RefSeq; NP_207837.2; NM_033401.4. [Q9C0A0-1]
DR RefSeq; NP_620481.2; NM_138994.4. [Q9C0A0-2]
DR PDB; 4NXQ; X-ray; 2.10 A; D/E/F=1301-1308.
DR PDBsum; 4NXQ; -.
DR AlphaFoldDB; Q9C0A0; -.
DR SMR; Q9C0A0; -.
DR BioGRID; 124532; 18.
DR DIP; DIP-31652N; -.
DR IntAct; Q9C0A0; 7.
DR MINT; Q9C0A0; -.
DR STRING; 9606.ENSP00000479811; -.
DR GlyGen; Q9C0A0; 12 sites.
DR iPTMnet; Q9C0A0; -.
DR PhosphoSitePlus; Q9C0A0; -.
DR BioMuta; CNTNAP4; -.
DR DMDM; 209572753; -.
DR EPD; Q9C0A0; -.
DR jPOST; Q9C0A0; -.
DR MassIVE; Q9C0A0; -.
DR PaxDb; Q9C0A0; -.
DR PeptideAtlas; Q9C0A0; -.
DR PRIDE; Q9C0A0; -.
DR ProteomicsDB; 20213; -.
DR ProteomicsDB; 79975; -. [Q9C0A0-1]
DR Antibodypedia; 30357; 183 antibodies from 26 providers.
DR DNASU; 85445; -.
DR Ensembl; ENST00000478060.5; ENSP00000418741.1; ENSG00000152910.19. [Q9C0A0-2]
DR Ensembl; ENST00000611870.5; ENSP00000479811.1; ENSG00000152910.19. [Q9C0A0-1]
DR GeneID; 85445; -.
DR KEGG; hsa:85445; -.
DR MANE-Select; ENST00000611870.5; ENSP00000479811.1; NM_033401.5; NP_207837.2.
DR UCSC; uc010chb.2; human. [Q9C0A0-1]
DR CTD; 85445; -.
DR DisGeNET; 85445; -.
DR GeneCards; CNTNAP4; -.
DR HGNC; HGNC:18747; CNTNAP4.
DR HPA; ENSG00000152910; Tissue enriched (brain).
DR MIM; 610518; gene.
DR neXtProt; NX_Q9C0A0; -.
DR OpenTargets; ENSG00000152910; -.
DR PharmGKB; PA134874662; -.
DR VEuPathDB; HostDB:ENSG00000152910; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000157674; -.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; Q9C0A0; -.
DR OMA; LSTQNWS; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q9C0A0; -.
DR TreeFam; TF321823; -.
DR PathwayCommons; Q9C0A0; -.
DR SignaLink; Q9C0A0; -.
DR BioGRID-ORCS; 85445; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; CNTNAP4; human.
DR GeneWiki; CNTNAP4; -.
DR GenomeRNAi; 85445; -.
DR Pharos; Q9C0A0; Tbio.
DR PRO; PR:Q9C0A0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9C0A0; protein.
DR Bgee; ENSG00000152910; Expressed in C1 segment of cervical spinal cord and 112 other tissues.
DR ExpressionAtlas; Q9C0A0; baseline and differential.
DR Genevisible; Q9C0A0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:2000821; P:regulation of grooming behavior; ISS:UniProtKB.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; ISS:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR028875; CASPR4.
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:SF40; PTHR15036:SF40; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1308
FT /note="Contactin-associated protein-like 4"
FT /id="PRO_0000019510"
FT TOPO_DOM 26..1241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1242..1262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1263..1308
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 212..364
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 398..547
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 549..586
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 587..792
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DOMAIN 793..957
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 958..997
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1046..1202
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1023
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1073
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 515..547
FT /evidence="ECO:0000250"
FT DISULFID 553..564
FT /evidence="ECO:0000250"
FT DISULFID 558..573
FT /evidence="ECO:0000250"
FT DISULFID 575..585
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..1202
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..28
FT /note="MGSVTGAVLKTLLLLSTQNWNRVEAGNS -> MWN (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_044464"
FT VAR_SEQ 310..357
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_044465"
FT VARIANT 276
FT /note="L -> V (in dbSNP:rs34251012)"
FT /id="VAR_061371"
FT VARIANT 513
FT /note="Q -> H (in dbSNP:rs6564343)"
FT /id="VAR_050268"
FT VARIANT 786
FT /note="Q -> R (in dbSNP:rs12933808)"
FT /evidence="ECO:0000269|PubMed:11214970, ECO:0000269|Ref.1"
FT /id="VAR_061372"
FT VARIANT 1155
FT /note="D -> E (in dbSNP:rs7202925)"
FT /evidence="ECO:0000269|PubMed:11214970, ECO:0000269|Ref.1"
FT /id="VAR_050269"
FT VARIANT 1300
FT /note="N -> S (in dbSNP:rs34198820)"
FT /id="VAR_050270"
FT CONFLICT 244
FT /note="L -> R (in Ref. 1; BAC55271)"
FT /evidence="ECO:0000305"
FT STRAND 1304..1307
FT /evidence="ECO:0007829|PDB:4NXQ"
SQ SEQUENCE 1308 AA; 145274 MW; C135FD64184E82B1 CRC64;
MGSVTGAVLK TLLLLSTQNW NRVEAGNSYD CDDPLVSALP QASFSSSSEL SSSHGPGFAR
LNRRDGAGGW SPLVSNKYQW LQIDLGERME VTAVATQGGY GSSNWVTSYL LMFSDSGWNW
KQYRQEDSIW GFSGNANADS VVYYRLQPSI KARFLRFIPL EWNPKGRIGM RIEVFGCAYR
SEVVDLDGKS SLLYRFDQKS LSPIKDIISL KFKTMQSDGI LLHREGPNGD HITLQLRRAR
LFLLINSGEA KLPSTSTLVN LTLGSLLDDQ HWHSVLIQRL GKQVNFTVDE HRHHFHARGE
FNLMNLDYEI SFGGIPAPGK SVSFPHRNFH GCLENLYYNG VDIIDLAKQQ KPQIIAMGNV
SFSCSQPQSM PVTFLSSRSY LALPDFSGEE EVSATFQFRT WNKAGLLLFS ELQLISGGIL
LFLSDGKLKS NLYQPGKLPS DITAGVELND GQWHSVSLSA KKNHLSVAVD GQMASAAPLL
GPEQIYSGGT YYFGGCPDKS FGSKCKSPLG GFQGCMRLIS ISGKVVDLIS VQQGSLGNFS
DLQIDSCGIS DRCLPNYCEH GGECSQSWST FHCNCTNTGY RGATCHNSIY EQSCEAYKHR
GNTSGFYYID SDGSGPLEPF LLYCNMTETA WTIIQHNGSD LTRVRNTNPE NPYAGFFEYV
ASMEQLQATI NRAEHCEQEF TYYCKKSRLV NKQDGTPLSW WVGRTNETQT YWGGSSPDLQ
KCTCGLEGNC IDSQYYCNCD ADRNEWTNDT GLLAYKEHLP VTKIVITDTG RLHSEAAYKL
GPLLCQGDRS FWNSASFDTE ASYLHFPTFH GELSADVSFF FKTTASSGVF LENLGIADFI
RIELRSPTVV TFSFDVGNGP FEISVQSPTH FNDNQWHHVR VERNMKEASL QVDQLTPKTQ
PAPADGHVLL QLNSQLFVGG TATRQRGFLG CIRSLQLNGM TLDLEERAQV TPEVQPGCRG
HCSSYGKLCR NGGKCRERPI GFFCDCTFSA YTGPFCSNEI SAYFGSGSSV IYNFQENYLL
SKNSSSHAAS FHGDMKLSRE MIKFSFRTTR TPSLLLFVSS FYKEYLSVII AKNGSLQIRY
KLNKYQEPDV VNFDFKNMAD GQLHHIMINR EEGVVFIEID DNRRRQVHLS SGTEFSAVKS
LVLGRILEHS DVDQDTALAG AQGFTGCLSA VQLSHVAPLK AALHPSHPDP VTVTGHVTES
SCMAQPGTDA TSRERTHSFA DHSGTIDDRE PLANAIKSDS AVIGGLIAVV IFILLCITAI
AVRIYQQKRL YKRSEAKRSE NVDSAEAVLK SELNIQNAVN ENQKEYFF
