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Contactin-5 (F11 axonin-1-related protein 2) (FAR-2)

 CNTN5_CHICK             Reviewed;        1027 AA.
Q90W79;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 104.
RecName: Full=Contactin-5;
AltName: Full=F11 axonin-1-related protein 2;
Short=FAR-2;
Flags: Precursor;
Name=CNTN5; Synonyms=FAR2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INTERACTION WITH NGCAM/L1 AND TNP.
TISSUE=Brain;
PubMed=11461156; DOI=10.1006/mcne.2001.1006;
Plagge A., Sendtner-Voelderndorff L., Sirim P., Freigang J., Rader C.,
Sonderegger P., Bruemmendorf T.;
"The contactin-related protein FAR-2 defines Purkinje cell clusters
and labels subpopulations of climbing fibers in the developing
cerebellum.";
Mol. Cell. Neurosci. 18:91-107(2001).
-!- FUNCTION: Contactins mediate cell surface interactions during
nervous system development. May contribute to the formation of
somatotopic maps of cerebellar afferents during the development of
the nervous system. {ECO:0000269|PubMed:11461156}.
-!- SUBUNIT: Interacts with INgCAM/L1 and the tenascin-R TNP protein.
Does not interacts with NrCAM. {ECO:0000269|PubMed:11461156}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed by subpopulations of Purkinje cells
in the cerebellum. Also also expressed by one type of Purkinje
cell afferents, the climbing fibers.
{ECO:0000269|PubMed:11461156}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
family. {ECO:0000305}.
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EMBL; AJ309935; CAC51431.1; -; mRNA.
RefSeq; NP_989943.1; NM_204612.1.
RefSeq; XP_015135375.1; XM_015279889.1.
UniGene; Gga.945; -.
ProteinModelPortal; Q90W79; -.
SMR; Q90W79; -.
STRING; 9031.ENSGALP00000027744; -.
PaxDb; Q90W79; -.
PRIDE; Q90W79; -.
Ensembl; ENSGALT00000050284; ENSGALP00000045880; ENSGALG00000017197.
GeneID; 395317; -.
KEGG; gga:395317; -.
CTD; 53942; -.
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00760000118840; -.
HOGENOM; HOG000059617; -.
HOVERGEN; HBG051047; -.
InParanoid; Q90W79; -.
KO; K06763; -.
PhylomeDB; Q90W79; -.
Reactome; R-GGA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
PRO; PR:Q90W79; -.
Proteomes; UP000000539; Chromosome 1.
ExpressionAtlas; Q90W79; baseline.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
CDD; cd00063; FN3; 4.
Gene3D; 2.60.40.10; -; 10.
InterPro; IPR032989; Contactin-5.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
PANTHER; PTHR43905:SF3; PTHR43905:SF3; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07679; I-set; 3.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 6.
SMART; SM00408; IGc2; 6.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 4.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein;
Membrane; Reference proteome; Repeat; Signal.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 999 Contactin-5.
/FTId=PRO_0000014725.
PROPEP 1000 1027 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000014726.
DOMAIN 32 117 Ig-like C2-type 1.
DOMAIN 123 209 Ig-like C2-type 2.
DOMAIN 227 307 Ig-like C2-type 3.
DOMAIN 317 401 Ig-like C2-type 4.
DOMAIN 407 494 Ig-like C2-type 5.
DOMAIN 498 593 Ig-like C2-type 6.
DOMAIN 600 698 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 703 800 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 805 899 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 901 994 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
COMPBIAS 1008 1013 Poly-Ser.
LIPID 999 999 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 376 376 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 467 467 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 706 706 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 743 743 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 858 858 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 929 929 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 100 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 144 196 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 249 296 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 338 385 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 430 478 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 520 577 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 1027 AA; 113048 MW; 62B6A11E544B4610 CRC64;
MMWLSWKLFL FLSLIGCLSE SVDYGPVFVQ EPDDVIFPTD SEEKKVSLNC QAHGSPTPTY
RWLRNGTEID VESDYRYSLI EGSLIISNPN EMKDSGQYQC LTTNMFGSIL SREAVLQFAY
LGNFSGRTRS AVSVREGQGV VLMCSPPLHS PEIIYSWVFN EFPSFVAEDS RRFISQETGN
LYISKVQTSD VGSYICLVKN TVTNARVLSP PTPLTLRNDG VMGEYEPKIE VHFPYTVTAA
RGTTVKMECF ALGNPVPTIS WKKVNGHNPS KARLRKSQAV LEIPNVQLED AGMYECKAEN
SRGRNVFRGQ LQVYTYPQWV EKLNDTELDS GEQLRWECKA TGKPRPTYRW LKNGVPLWPQ
SRIEMINSVL MIRTVNISDA GMYQCLAENK YGTIYASAEL KILASAPTFP LNQMRKTIII
TKGQEVVIEC KPQASPKPTI TWKKGDKALR ESKRVTILPQ GSLRILNASK SDEGRYSCRG
VNVFGSAEIV ASVSVKEPTR IELTPKKIEL TVGESIVLSC KALHDSTLDV TFYWTLNGQP
IDFDKEDGHF ESIKAQASSA DLMIRNILLM HAGRYGCRVQ TAADAVSDET ELLVRGPPGP
PGVVIVEEIT DTTATLSWSP GADNHSPISL YNLQARSPFS LGWQTVKTVP DVISGDMESA
MAVELNPWVE YEFRVVATNK IGTGDPSAPS RMIRTNEAVP KTPPANVSGR SGRRHELVIA
WEPVSEEFQN GEGFGYIVAF RPNGTRGWKE KMVTSSDASK FIYRDESVPP LTPFEVKVGV
YNNKGDGPFS PIVVICSAEG EPTAAPIDVK ATSLSVSEIL VAWKHIKESL GRPQGFEIGY
WKDMEQEEAA EKVKTAGNES SLLLTGLEGN TLYHLTVRAY NAAGYGPPST AVRVATKKSP
PSQAPSNVMW IQDGSHVSLG WEPVRPLANE SEVMGYKVLL RQEGQSNSQV IETQKTSAVV
ILPDVGVYII EVCAVSEGGD GTASPQIRVP SYAGGKVTSA QSTLHMFSTS SSSVTLLLVL
MVPSTSW


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