ID A0A287BG37_PIG Unreviewed; 1038 AA.
AC A0A287BG37;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Contactin 2 {ECO:0000313|Ensembl:ENSSSCP00000055015.2};
GN Name=CNTN2 {ECO:0000313|Ensembl:ENSSSCP00000055015.2,
GN ECO:0000313|VGNC:VGNC:108577};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000055015.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000055015.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000055015.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000055015.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000256|ARBA:ARBA00009812}.
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DR AlphaFoldDB; A0A287BG37; -.
DR SMR; A0A287BG37; -.
DR STRING; 9823.ENSSSCP00000055015; -.
DR Ensembl; ENSSSCT00000045904.3; ENSSSCP00000055015.2; ENSSSCG00000040824.3.
DR VGNC; VGNC:108577; CNTN2.
DR GeneTree; ENSGT00940000159193; -.
DR InParanoid; A0A287BG37; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000040824; Expressed in prefrontal cortex and 13 other cell types or tissues.
DR ExpressionAtlas; A0A287BG37; baseline.
DR GO; GO:0043194; C:axon initial segment; IEA:Ensembl.
DR GO; GO:0044224; C:juxtaparanode region of axon; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; IEA:Ensembl.
DR GO; GO:0071206; P:establishment of protein localization to juxtaparanode region of axon; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0097090; P:presynaptic membrane organization; IEA:Ensembl.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
DR CDD; cd05727; Ig2_Contactin-2-like; 1.
DR CDD; cd04969; Ig5_Contactin; 1.
DR CDD; cd05850; IgI_1_Contactin-2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR InterPro; IPR047102; Contactin-1_2_Ig1.
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:SF28; CONTACTIN-2; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1038
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023893165"
FT DOMAIN 43..128
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 133..222
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 239..322
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 327..411
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 417..504
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 509..603
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 610..707
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 712..809
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 814..909
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 693..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 112951 MW; 92B04106A0B23360 CRC64;
MGTARRRKSH LLLLVAVVLV SAPAWSSARG SQATFGPVFE DQPLGLLFPE ESTEEKVTLA
CRARASPPAT YRWKMNGTEM KLEPGSRHQL VGGNLVIMNP TKAQDAGVYQ CLASNPVGTV
VSREAVLRFG FLQEFSKEER DPVKTHEGWG VMLPCNPPAH YPGLSYRWLL NEFPNFIPTD
GRHFVSQTTG NLYIARTNAS DLGNYSCLAT SHMDFSTKSV FSKFAQLNLA AEDTRLFAPS
IKAKFPAETY ALVGQQVTLE CFAFGNPVPR IKWRKVDGSL SPQWATAEPT LQIPSVGFED
EGTYECEAEN SKGRDTVQGR IIVQAQPEWL KVISDMEADI GSNLHWGCAA AGKPRPTVRW
LRNGEPLASQ ARVEVMAGDL RFSKLSLEDS GMYQCVAENK HGTIYASAEL AVQALAPDFR
LNPVRRLIPA ARGGEIIIPC QPRAAPKAVV LWSKGTEILV NSSRVTVTPD GTLIIRNISR
SDEGKYTCFA ENFMGKANST GILSVRDATK ITLAPSSADI NLGDNLTLQC HASHDPTMDL
TFIWMLDDFP IDFDKPGGHY RRASVKETVG DLSILNAQLR HGGKYTCMAQ TVVDSASKEA
TVLVRGPPGP PGGVVVREIG DTTVQLSWSR GFDNHSPIAK YTLQARTLPG KWKQVRTNPA
NIEGNAETAQ VLGLTPWMDY EFRVVASNIL GTGEPSGPSS KIRTKEAAPS VAPSGLSGGG
GAPGELIVNW TPMSREYQNG DGFGYLLSFR RQGSTSWQTA RVPGADAQYF VYSNESVRPY
TPFEVKIRSY NRRGEGPESL TALVYSAEEE PRVAPTKVWA QGVASSEMNV TWEPVQQDMN
GILLGYEIRY WKAGDKEAAA DRVRTAGLDT TALVTGLHPN TKYHVTVRAY NRAGTGPASP
AANATTMKPP PRRPPGNISW TFSSSSLSIK WDPVVALRNE SAVTGYKMLY QNDLHPPTLH
LTNKNWIEIA VPEDIGHALV QIRTTGPGGD GVPAEVHIVK NGGTSMMVEN SAVSPAPHPG
TVLSHSVVTL ILIGYLEL
//
