CNTN5_CHICK
ID CNTN5_CHICK Reviewed; 1027 AA.
AC Q90W79;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Contactin-5;
DE AltName: Full=F11 axonin-1-related protein 2;
DE Short=FAR-2;
DE Flags: Precursor;
GN Name=CNTN5; Synonyms=FAR2;
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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH NGCAM/L1 AND TNP.
RC TISSUE=Brain;
RX PubMed=11461156; DOI=10.1006/mcne.2001.1006;
RA Plagge A., Sendtner-Voelderndorff L., Sirim P., Freigang J., Rader C.,
RA Sonderegger P., Bruemmendorf T.;
RT "The contactin-related protein FAR-2 defines Purkinje cell clusters and
RT labels subpopulations of climbing fibers in the developing cerebellum.";
RL Mol. Cell. Neurosci. 18:91-107(2001).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. May contribute to the formation of somatotopic maps
CC of cerebellar afferents during the development of the nervous system.
CC {ECO:0000269|PubMed:11461156}.
CC -!- SUBUNIT: Interacts with INgCAM/L1 and the tenascin-R TNP protein. Does
CC not interacts with NrCAM. {ECO:0000269|PubMed:11461156}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by subpopulations of Purkinje cells in
CC the cerebellum. Also expressed by one type of Purkinje cell afferents,
CC the climbing fibers. {ECO:0000269|PubMed:11461156}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; AJ309935; CAC51431.1; -; mRNA.
DR RefSeq; NP_989943.1; NM_204612.1.
DR RefSeq; XP_015135375.1; XM_015279889.1.
DR AlphaFoldDB; Q90W79; -.
DR SMR; Q90W79; -.
DR STRING; 9031.ENSGALP00000027744; -.
DR PaxDb; Q90W79; -.
DR PRIDE; Q90W79; -.
DR Ensembl; ENSGALT00000050284; ENSGALP00000045880; ENSGALG00000017197.
DR GeneID; 395317; -.
DR KEGG; gga:395317; -.
DR CTD; 53942; -.
DR VEuPathDB; HostDB:geneid_395317; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000158183; -.
DR InParanoid; Q90W79; -.
DR PhylomeDB; Q90W79; -.
DR PRO; PR:Q90W79; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000017197; Expressed in brain and 2 other tissues.
DR ExpressionAtlas; Q90W79; baseline and differential.
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 CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR032989; Contactin-5.
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:SF17; PTHR44170:SF17; 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; 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 Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..999
FT /note="Contactin-5"
FT /id="PRO_0000014725"
FT PROPEP 1000..1027
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014726"
FT DOMAIN 32..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 123..209
FT /note="Ig-like C2-type 2"
FT DOMAIN 227..307
FT /note="Ig-like C2-type 3"
FT DOMAIN 317..401
FT /note="Ig-like C2-type 4"
FT DOMAIN 407..494
FT /note="Ig-like C2-type 5"
FT DOMAIN 498..593
FT /note="Ig-like C2-type 6"
FT DOMAIN 600..698
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 703..800
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 805..899
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 901..994
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT LIPID 999
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 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
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 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 249..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 338..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 430..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 520..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ 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
