CNTN4_RAT
ID CNTN4_RAT Reviewed; 1026 AA.
AC Q62845;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Contactin-4;
DE AltName: Full=Brain-derived immunoglobulin superfamily protein 2;
DE Short=BIG-2;
DE Flags: Precursor;
GN Name=Cntn4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8586965; DOI=10.1002/neu.480280106;
RA Yoshihara Y., Kawasaki M., Tamada A., Nagata S., Kagamiyama H., Mori K.;
RT "Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3:
RT four members of an axon-associated cell adhesion molecule subgroup of the
RT immunoglobulin superfamily.";
RL J. Neurobiol. 28:51-69(1995).
RN [2]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16806532; DOI=10.1016/j.bbaexp.2006.04.008;
RA Radom J., Colin D., Thiebault F., Dognin-Bergeret M.J., Mairet-Coello G.,
RA Esnard-Feve A., Fellmann D., Jouvenot M.;
RT "Identification and expression of a new splicing variant of FAD-sulfhydryl
RT oxidase in adult rat brain.";
RL Biochim. Biophys. Acta 1759:225-233(2006).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Has some neurite outgrowth-promoting activity. May
CC be involved in synaptogenesis. {ECO:0000269|PubMed:8586965}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Secreted {ECO:0000269|PubMed:16806532}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the nervous system. Not
CC expressed in heart, spleen, lung, liver, kidney or skeletal muscle. In
CC the hippocampus, it is highly expressed in CA1 pyramidal cells and
CC weakly expressed in other regions of the hippocampus.
CC {ECO:0000269|PubMed:8586965}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; U35371; AAC52262.1; -; mRNA.
DR RefSeq; NP_446331.1; NM_053879.1.
DR RefSeq; XP_017447884.1; XM_017592395.1.
DR RefSeq; XP_017447885.1; XM_017592396.1.
DR AlphaFoldDB; Q62845; -.
DR SMR; Q62845; -.
DR STRING; 10116.ENSRNOP00000007788; -.
DR GlyGen; Q62845; 13 sites.
DR PhosphoSitePlus; Q62845; -.
DR PaxDb; Q62845; -.
DR PRIDE; Q62845; -.
DR Ensembl; ENSRNOT00000007788; ENSRNOP00000007788; ENSRNOG00000005652.
DR GeneID; 116658; -.
DR KEGG; rno:116658; -.
DR CTD; 152330; -.
DR RGD; 621361; Cntn4.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000155198; -.
DR InParanoid; Q62845; -.
DR OMA; KICKAYT; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q62845; -.
DR TreeFam; TF351103; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q62845; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000005652; Expressed in frontal cortex and 2 other tissues.
DR ExpressionAtlas; Q62845; baseline and differential.
DR Genevisible; Q62845; RN.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:UniProtKB.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
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 PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1000
FT /note="Contactin-4"
FT /id="PRO_0000014715"
FT PROPEP 1001..1026
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014716"
FT DOMAIN 32..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..206
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..311
FT /note="Ig-like C2-type 3"
FT DOMAIN 316..400
FT /note="Ig-like C2-type 4"
FT DOMAIN 406..493
FT /note="Ig-like C2-type 5"
FT DOMAIN 497..586
FT /note="Ig-like C2-type 6"
FT DOMAIN 599..697
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 702..799
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 804..899
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 900..995
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 685..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1000
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 247..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 337..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 429..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 519..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1026 AA; 113393 MW; B60C0EEFA17BE3CC CRC64;
MRLPWELLVL QSFMLCLADD YTLHGPVFVQ EPSHVMFPLD SEEKKVKLSC EVKGNPKPHI
RWKLNGTDVD IGMDFRYSVV EGSLLINNPN KTQDSGTYQC IATNSFGTIV SREAKLQFAY
LENFKTRTRS TVSVRRGQGM VLLCGPPPHS GELSYAWIFN EHPSYQDNRR FVSQETGNLY
IAKVEKADVG NYTCVVTNTV TSHQVLGPPT PLILRNDGVM GEYEPKIEVQ FPETVPAEKG
STVKLECFAL GNPVPTILWR RADGKPIARK ARRHKSSGIL EIPNFQQEDA GSYECVAENS
RGKNIAKGQV TFYAQPNWVQ IINDIHVAME ESVFWECKAN GRPKPTYRWL KNGDPLLTRE
RIQIEQGTLN ITIVNLSDAG MYQCVAENKH GVIYASAELS VIAESPDFSR TLLKRVTLVK
VGGEVVIECK PKASPRPVYT WRKGREILRE NERITISEDG NLRIINVTKS DAGSYTCIAT
NHFGTASSTG NVVVKDPTKV MVPPSSMDVT VGESIVLPCQ VTHDHSLDIV FTWTFNGHLI
DFDKDGDHFE RVGGQDSAGD LMIRNIQLKH AGKYVCMVQT SVDKLSAAAD LIVRGPPGPP
EAVTIDEITD TTAQLSWRPG PDNHSPITMY VIQARTPFSV GWQAVSTVPE LVDGKTFTAT
VVGLNPWVEY EFRTVAANVI GIGEPSRPSE KRRTEEALPE VTPANVSGGG GSKSELVITW
ETVPEELQNG RGFGYVVAFR PHGKMIWMLT VLASADASRY VFRNESVRPF SPFEVKVGVF
NNKGEGPFSP TTLVYSAEEE PTKPPASIFA RSLSATDIEV FWASPIGKNR GRIQGYEVKY
WRHDDKEENA RKIRTVGNQT STKITNLKGN ALYHLSVKAY NSAGTGPSSA AVNVTTRKPP
PSQPPGNIIW NSSDSKIILN WDQVKALDNE SEVKGYKVLY RWNRQSSTSV IETNKTSVEL
SLPFDEDYII EIKPFSDGGD GSSSEQIRIP KISNSYARGS GASTSNACTL SAISTIMISL
TARSSL
