CNTN1_CHICK
ID CNTN1_CHICK Reviewed; 1010 AA.
AC P14781; P10450;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Contactin-1;
DE AltName: Full=Neural cell recognition molecule F11;
DE Flags: Precursor;
GN Name=CNTN1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2627374; DOI=10.1016/0896-6273(89)90073-1;
RA Bruemmendorf T., Wolff J.M., Rainer F., Rathjer F.G.;
RT "Neural cell recognition molecule F11: homology with fibronectin type III
RT and immunoglobulin type C domains.";
RL Neuron 2:1351-1361(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RX PubMed=3049624; DOI=10.1083/jcb.107.4.1561;
RA Ranscht B., Dours M.T.;
RT "Sequence of contactin, a 130-kD glycoprotein concentrated in areas of
RT interneuronal contact, defines a new member of the immunoglobulin supergene
RT family in the nervous system.";
RL J. Cell Biol. 107:1561-1573(1988).
RN [3]
RP GPI-ANCHOR.
RX PubMed=2735929; DOI=10.1016/0006-291x(89)92688-0;
RA Wolff J.M., Bruemmendorf T., Rathjen F.G.;
RT "Neural cell recognition molecule F11: membrane interaction by covalently
RT attached phosphatidylinositol.";
RL Biochem. Biophys. Res. Commun. 161:931-938(1989).
RN [4]
RP INTERACTION WITH TNR, AND FUNCTION.
RX PubMed=7615642; DOI=10.1083/jcb.130.2.473;
RA Noerenberg U., Hubert M., Bruemmendorf T., Tarnok A., Rathjen F.G.;
RT "Characterization of functional domains of the tenascin-R (restrictin)
RT polypeptide: cell attachment site, binding with F11, and enhancement of
RT F11-mediated neurite outgrowth by tenascin-R.";
RL J. Cell Biol. 130:473-484(1995).
CC -!- FUNCTION: Mediates cell surface interactions during nervous system
CC development. Interaction with TNR enhances the neurite outgrowth.
CC {ECO:0000269|PubMed:7615642}.
CC -!- SUBUNIT: Interacts with TNR. {ECO:0000269|PubMed:7615642}.
CC -!- INTERACTION:
CC P14781; F1NPE8: PTPRA; NbExp=2; IntAct=EBI-2123196, EBI-7140740;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68753.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X14877; CAA33018.1; -; mRNA.
DR EMBL; Y00813; CAA68753.1; ALT_FRAME; mRNA.
DR PIR; S01998; S01998.
DR RefSeq; NP_001004381.3; NM_001004381.3.
DR PDB; 5E53; X-ray; 2.50 A; A/B/C/D=593-893.
DR PDBsum; 5E53; -.
DR AlphaFoldDB; P14781; -.
DR SMR; P14781; -.
DR BioGRID; 679083; 1.
DR IntAct; P14781; 3.
DR MINT; P14781; -.
DR STRING; 9031.ENSGALP00000038042; -.
DR PaxDb; P14781; -.
DR Ensembl; ENSGALT00000038834; ENSGALP00000038042; ENSGALG00000009523.
DR Ensembl; ENSGALT00000075780; ENSGALP00000050725; ENSGALG00000009523.
DR GeneID; 417786; -.
DR KEGG; gga:417786; -.
DR CTD; 1272; -.
DR VEuPathDB; HostDB:geneid_417786; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000155915; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; P14781; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; P14781; -.
DR PRO; PR:P14781; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000009523; Expressed in cerebellum and 12 other tissues.
DR ExpressionAtlas; P14781; baseline.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
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; 3.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
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 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT CHAIN 20..984
FT /note="Contactin-1"
FT /id="PRO_0000014691"
FT PROPEP 985..1010
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014692"
FT DOMAIN 33..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 132..215
FT /note="Ig-like C2-type 2"
FT DOMAIN 232..317
FT /note="Ig-like C2-type 3"
FT DOMAIN 322..398
FT /note="Ig-like C2-type 4"
FT DOMAIN 404..491
FT /note="Ig-like C2-type 5"
FT DOMAIN 496..592
FT /note="Ig-like C2-type 6"
FT DOMAIN 597..695
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 700..797
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 802..897
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 899..990
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 679..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 984
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 924
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 254..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 343..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 427..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 517..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 971
FT /note="S -> N (in Ref. 2; CAA68753)"
FT /evidence="ECO:0000305"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 608..615
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 655..661
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 667..673
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 702..706
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 713..719
FT /evidence="ECO:0007829|PDB:5E53"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 728..730
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 732..739
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 746..750
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 757..761
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 770..779
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 790..793
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 804..810
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 812..814
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 816..821
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 830..837
FT /evidence="ECO:0007829|PDB:5E53"
FT HELIX 842..844
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 846..851
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 855..859
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 867..870
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 873..876
FT /evidence="ECO:0007829|PDB:5E53"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:5E53"
SQ SEQUENCE 1010 AA; 112507 MW; 2E38F071AF423AE1 CRC64;
MRFFISHLVT LCFIFCVADS THFSEEGNKG YGPVFEEQPI DTIYPEESSD GQVSMNCRAR
AVPFPTYKWK LNNWDIDLTK DRYSMVGGRL VISNPEKSRD AGKYVCVVSN IFGTVRSSEA
TLSFGYLDPF PPEEHYEVKV REGVGAVLLC EPPYHYPDDL SYRWLLNEFP VFIALDRRRF
VSQTNGNLYI ANVEASDKGN YSCFVSSPSI TKSVFSKFIP LIPQADRAKV YPADIKVKFK
DTYALLGQNV TLECFALGNP VPELRWSKYL EPMPATAEIS MSGAVLKIFN IQYEDEGLYE
CEAENYKGKD KHQARVYVQA SPEWVEHIND TEKDIGSDLY WPCVATGKPI PTIRWLKNGV
SFRKGELRIQ GLTFEDAGMY QCIAENAHGI IYANAELKIV ASPPTFELNP MKKKILAAKG
GRVIIECKPK AAPKPKFSWS KGTELLVNGS RIHIWDDGSL EIINVTKLDE GRYTCFAENN
RGKANSTGVL EMTEATRITL APLNVDVTVG ENATMQCIAS HDPTLDLTFI WSLNGFVIDF
EKEHEHYERN VMIKSNGELL IKNVQLRHAG RYTCTAQTIV DNSSASADLV VRGPPGPPGG
IRIEEIRDTA VALTWSRGTD NHSPISKYTI QSKTFLSEEW KDAKTEPSDI EGNMESARVI
DLIPWMEYEF RIIATNTLGT GEPSMPSQRI RTEGAPPNVA PSDVGGGGGS NRELTITWMP
LSREYHYGNN FGYIVAFKPF GEKEWRRVTV TNPEIGRYVH KDESMPPSTQ YQVKVKAFNS
KGDGPFSLTA VIYSAQDAPT EVPTDVSVKV LSSSEISVSW HHVTEKSVEG YQIRYWAAHD
KEAAAQRVQV SNQEYSTKLE NLKPNTRYHI DVSAFNSAGY GPPSRTIDII TRKAPPSQRP
RIISSVRSGS RYIITWDHVK AMSNESAVEG YKVLYRPDGQ HEGKLFSTGK HTIEVPVPSD
GEYVVEVRAH SEGGDGEVAQ IKISGATAGV PTLLLGLVLP ALGVLAYSGF
