CNTN1_BOVIN
ID CNTN1_BOVIN Reviewed; 1018 AA.
AC Q28106;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Contactin-1;
DE AltName: Full=Neural cell surface protein F3;
DE Flags: Precursor;
GN Name=CNTN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7642103; DOI=10.1016/0378-1119(95)00062-b;
RA Watanabe K., Shimazaki K., Hosoya H., Fukamauchi F., Takenawa T.;
RT "Cloning of the DNA encoding neural adhesion molecule F3 from bovine
RT brain.";
RL Gene 160:245-248(1995).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Involved in the formation of paranodal axo-glial
CC junctions in myelinated peripheral nerves and in the signaling between
CC axons and myelinating glial cells via its association with CNTNAP1.
CC Participates in oligodendrocytes generation by acting as a ligand of
CC NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through
CC the released notch intracellular domain (NICD) and subsequent
CC translocation to the nucleus. Interaction with TNR induces a repulsion
CC of neurons and an inhibition of neurite outgrowth (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with CNTNAP1 in cis form (By similarity).
CC Binds to the carbonic-anhydrase like domain of PTPRZ1. Interacts with
CC NOTCH1 and TNR. Detected in a complex with NRCAM and PTPRB (By
CC similarity). Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:P12960, ECO:0000250|UniProtKB:Q12860,
CC ECO:0000250|UniProtKB:Q63198}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; D32135; BAA06861.1; -; mRNA.
DR PIR; JC4211; JC4211.
DR RefSeq; NP_776705.1; NM_174280.2.
DR AlphaFoldDB; Q28106; -.
DR SMR; Q28106; -.
DR STRING; 9913.ENSBTAP00000042896; -.
DR PaxDb; Q28106; -.
DR PRIDE; Q28106; -.
DR GeneID; 281705; -.
DR KEGG; bta:281705; -.
DR CTD; 1272; -.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; Q28106; -.
DR OrthoDB; 655902at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR036992; Contactin-1.
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; PTHR44170:SF10; PTHR44170:SF10; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 2.
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 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Notch signaling pathway;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..999
FT /note="Contactin-1"
FT /id="PRO_0000014683"
FT PROPEP 1000..1018
FT /note="Removed in mature form"
FT /id="PRO_0000014684"
FT DOMAIN 41..131
FT /note="Ig-like C2-type 1"
FT DOMAIN 137..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 241..326
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..407
FT /note="Ig-like C2-type 4"
FT DOMAIN 413..500
FT /note="Ig-like C2-type 5"
FT DOMAIN 504..601
FT /note="Ig-like C2-type 6"
FT DOMAIN 606..704
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 709..806
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 811..906
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 907..1000
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 698..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 999
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 263..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 436..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 526..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1018 AA; 113385 MW; 551FC10ED7920341 CRC64;
MKMWLLFSLL VIISFKTCLS EFTWHRRYGH GVSEEDKGFG PIFEEQPINT IYPEESPEGK
VSLNCRARAS PFPVYKWRMN NGDIDLTSDR YSMVGGNLVI NNPDKQKDAG IYYCLASNNY
GMVRSTEATL SFGYLDPFPP EERPEVRVKE GKGMVLLCDP PYHFPDDLSY RWLLNEFPVF
ITMDKRRFVS QTNGNLYIAN VEASDKGNYS CFVSSPSITK SVFSKFIPLI PLPERTTKPY
PADIVVQFKD VYALMGQNVT LECFALGNPV PDIRWRKVLE PMPSTAEIST SGAVLKIFNI
QLEDEGIYEC EAENNRGKDK HQARIYVQAF PEWVEHINDT EVDIGSDLYW PCVATGKPIP
TIRWLKNGYS YHRGELRLYD VTFENAGMYQ CIAENTHGAI YANAELKILA LAPTFEMNPM
KKKILAAKGG RVIIECKPKA APKPTFLWSK GTERLVNSSR ILIWEDGSLE INNITRSDGG
VYTCFVENNK GKANSTGTLV ITDPTRIILA PINADITVGE NATMQCAASF DPALDLTFVW
SFNGYVIDFN KENIHYQRNF MLDSNGELLI RNAQLKHAGR YTCTAQTIVD NSSASADLVV
RGPPGPPGGL RIEDIRATSV ALTWSRGSDN HSPISKYTIQ TKTILSDDWK DAKTDPPIIE
GNMEAARAVD LIPWMEYEFR VVATNTLGIG EPSIPSNKIK TDGAAPNVAP SDVGGGGGSN
RELTITWAPL SREYHYFNNF GYIVAFKPFD GEEWKKVTVT NPDTGRYVHK DETMRPSTAF
QVKVKAFNNK GDGPYSLTAV IHSAQDAPSE APTAVGVKVL SSSEISVHWE HVVEKIVESY
QIRYWASHDK EAAAHRVQVA SQEYSARLEN LLPDTQYFVE VRACNSAGCG PPSDMTETFT
KKAPPSQPPR IISSVRSGSR YIITWDHVVA LSNESTVTGY KVLYRPDGQH DGKLYSTHKH
SIEVPIPRDG EYVVEVRAHS DGGDGVVSQV KISGASILSP CLLGFLLPAL GILVYLEF
