CNTN2_CHICK
ID CNTN2_CHICK Reviewed; 1036 AA.
AC P28685;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Contactin-2;
DE AltName: Full=Axonin-1;
DE Flags: Precursor;
GN Name=CNTN2;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1311675; DOI=10.1111/j.1432-1033.1992.tb16655.x;
RA Zuellig R.A., Rader C., Schroeder A., Kalousek M.B.,
RA von Bohlen Und Halbach F., Osterwalder T., Inan C., Stoeckli E.T.,
RA Affolter H.-U., Fritz A., Hafen E., Sonderegger P.;
RT "The axonally secreted cell adhesion molecule, axonin-1. Primary structure,
RT immunoglobulin-like and fibronectin-type-III-like domains and glycosyl-
RT phosphatidylinositol anchorage.";
RL Eur. J. Biochem. 204:453-463(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7867620; DOI=10.1111/j.1432-1033.1995.tb20181.x;
RA Giger R.J., Vogt L., Zuellig R.A., Rader C., Henehan-Beatty A.,
RA Wolfer D.P., Sonderegger P.;
RT "The gene of chicken axonin-1. Complete structure and analysis of the
RT promoter.";
RL Eur. J. Biochem. 227:617-628(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 28-409, AND DISULFIDE BONDS.
RX PubMed=10830169; DOI=10.1016/s0092-8674(00)80852-1;
RA Freigang J., Proba K., Leder L., Diederichs K., Sonderegger P., Welte W.;
RT "The crystal structure of the ligand binding module of axonin-1/TAG-1
RT suggests a zipper mechanism for neural cell adhesion.";
RL Cell 101:425-433(2000).
CC -!- FUNCTION: Axon-associated cell adhesion molecule (AxCAM) which promotes
CC neurite outgrowth by interaction with the AxCAM L1 (G4) of neuritic
CC membrane. Contributes to the organization of axonal domains at nodes of
CC Ranvier (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Note=Attached to the neuronal membrane by a GPI-anchor.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X63101; CAA44815.1; -; mRNA.
DR EMBL; X79607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S22383; S22383.
DR RefSeq; NP_001004395.1; NM_001004395.1.
DR PDB; 1CS6; X-ray; 1.80 A; A=28-409.
DR PDBsum; 1CS6; -.
DR AlphaFoldDB; P28685; -.
DR SMR; P28685; -.
DR STRING; 9031.ENSGALP00000000926; -.
DR PaxDb; P28685; -.
DR GeneID; 419825; -.
DR KEGG; gga:419825; -.
DR CTD; 6900; -.
DR VEuPathDB; HostDB:geneid_419825; -.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; P28685; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; P28685; -.
DR EvolutionaryTrace; P28685; -.
DR PRO; PR:P28685; -.
DR Proteomes; UP000000539; Unplaced.
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:0050839; F:cell adhesion molecule binding; IPI:AgBase.
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 GO; GO:0007158; P:neuron cell-cell adhesion; IDA:AgBase.
DR GO; GO:0097090; P:presynaptic membrane organization; ISS:UniProtKB.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 10.
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 Pfam; PF00041; fn3; 3.
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; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..23
FT /note="Or 25"
FT /evidence="ECO:0000255"
FT CHAIN 24..?
FT /note="Contactin-2"
FT /id="PRO_0000014701"
FT PROPEP ?..1036
FT /note="Removed in mature form"
FT /id="PRO_0000014702"
FT DOMAIN 32..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 234..317
FT /note="Ig-like C2-type 3"
FT DOMAIN 322..406
FT /note="Ig-like C2-type 4"
FT DOMAIN 412..499
FT /note="Ig-like C2-type 5"
FT DOMAIN 504..598
FT /note="Ig-like C2-type 6"
FT DOMAIN 605..703
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 708..805
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 810..907
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 911..1003
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 599..608
FT /note="Hinge"
FT /evidence="ECO:0000255"
FT REGION 889..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..106
FT /evidence="ECO:0000269|PubMed:10830169,
FT ECO:0007744|PDB:1CS6"
FT DISULFID 150..202
FT /evidence="ECO:0000269|PubMed:10830169,
FT ECO:0007744|PDB:1CS6"
FT DISULFID 256..301
FT /evidence="ECO:0000269|PubMed:10830169,
FT ECO:0007744|PDB:1CS6"
FT DISULFID 343..390
FT /evidence="ECO:0000269|PubMed:10830169,
FT ECO:0007744|PDB:1CS6"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:1CS6"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1CS6"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1CS6"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:1CS6"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 308..326
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:1CS6"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:1CS6"
FT STRAND 397..408
FT /evidence="ECO:0007829|PDB:1CS6"
SQ SEQUENCE 1036 AA; 113302 MW; 08B80143BE779794 CRC64;
MGGTAAFICT SLAVIICVVW CQAQSGMRSY GPVFEEQPAH TLFPEGSAEE KVTLTCRARA
NPPATYRWKM NGTELKMGPD SRYRLVAGDL VISNPVKAKD AGSYQCVATN ARGTVVSREA
SLRFGFLQEF SAEERDPVKI TEGWGVMFTC SPPPHYPALS YRWLLNEFPN FIPADGRRFV
SQTTGNLYIA KTEASDLGNY SCFATSHIDF ITKSVFSKFS QLSLAAEDAR QYAPSIKAKF
PADTYALTGQ MVTLECFAFG NPVPQIKWRK LDGSQTSKWL SSEPLLHIQN VDFEDEGTYE
CEAENIKGRD TYQGRIIIHA QPDWLDVITD TEADIGSDLR WSCVASGKPR PAVRWLRDGQ
PLASQNRIEV SGGELRFSKL VLEDSGMYQC VAENKHGTVY ASAELTVQAL APDFRLNPVK
RLIPAARSGK VIIPCQPRAA PKATVLWTKG TELLTNSSRV TITADGTLIL QNISKSDEGK
YTCFAENFMG KANSTGILSV RDATKITLAP SSADINVGEN LTLQCHASHD PTMDLTFTWS
LDDFPIDLDK SEGHYRRASV KEAVGDLAIV NAQLKHSGRY TCTAQTVVDS TSESATLTVR
GPPGPPGGVV VRDIGDTTVQ LSWSRGFDNH SPIARYSIEA RTLLSNKWKQ MRTNPVNIEG
NAETAQVVNL IPWMDYEFRV LASNILGVGE PSLPSSKIRT KEAAPTVAPS GLGGGGGAPN
ELIINWTPTL RDYQNGDGFG YILSFRKKGT QGWLTARVPH AESLHYVYRN ESIGPYTPFE
VKIKAYNRKG EGPESLTAIV YSAEEEPKVA PFRVTAKAVL SSEMDVSWEP VEQGDMTGVL
LGYEIRYWKD GDKEEAADRV RTAGLVTSAH VTGLNPNTKY HVSVRAYNRA GAGPPSPSTN
ITTTKPPPRR PPGNISWTLT GSTVTIKWDP VVAQADESAV TGYKMLYRQD SHSAPTLYLA
SKSRIDIPVP EDFTHAFVQI RVTGPGGDGT PAEVHIVRNS GTSMMVEDSV TRPVPHAAII
TTNSLAMVAL IRYLEL
