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T-lymphocyte activation antigen CD86 (Activation B7-2 antigen) (B70) (BU63) (CTLA-4 counter-receptor B7.2) (FUN-1) (CD antigen CD86)

 CD86_HUMAN              Reviewed;         329 AA.
P42081; A0N0P0; B7Z2F3; B7Z702; E7ETN5; E9PC27; Q13655; Q6FHB1;
Q6GTS4; Q7M4L5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
12-SEP-2018, entry version 184.
RecName: Full=T-lymphocyte activation antigen CD86;
AltName: Full=Activation B7-2 antigen;
AltName: Full=B70;
AltName: Full=BU63;
AltName: Full=CTLA-4 counter-receptor B7.2;
AltName: Full=FUN-1;
AltName: CD_antigen=CD86;
Flags: Precursor;
Name=CD86; Synonyms=CD28LG2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ILE-185.
PubMed=7694153; DOI=10.1038/366076a0;
Azuma M., Ito D., Yagita K., Okumura K., Phillips J.H., Lanier L.L.,
Somoza C.;
"B70 antigen is a second ligand for CTLA-4 and CD28.";
Nature 366:76-79(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-185.
PubMed=7694363; DOI=10.1126/science.7694363;
Freeman G.J., Gribben J.G., Boussiotis V.A., Ng J.W.,
Restivo V.A. Jr., Lombard L.A., Gray G.S., Nadler L.M.;
"Cloning of B7-2: a CTLA-4 counter-receptor that costimulates human T
cell proliferation.";
Science 262:909-911(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND VARIANT ILE-185.
PubMed=11162656; DOI=10.1006/bbrc.2000.4102;
Magistrelli G., Caron G., Gauchat J.-F., Jeannin P., Bonnefoy J.-Y.,
Delneste Y.;
"Identification of an alternatively spliced variant of human CD86
mRNA.";
Biochem. Biophys. Res. Commun. 280:1211-1215(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ILE-185.
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-185.
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANTS
ILE-185 AND THR-310.
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ILE-185 AND THR-310.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-329, AND VARIANT ILE-185.
TISSUE=Foreskin;
PubMed=7541777; DOI=10.1007/BF00178582;
Jellis C.L., Wang S.S., Rennert P., Borriello F., Sharpe A.H.,
Green N.R., Gray G.S.;
"Genomic organization of the gene coding for the costimulatory human
B-lymphocyte antigen B7-2 (CD86).";
Immunogenetics 42:85-89(1995).
[10]
CHARACTERIZATION.
PubMed=7527824;
Lanier L.L., O'Fallon S., Somoza C., Phillips J.H., Linsley P.S.,
Okumura K., Ito D., Azuma M.;
"CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T
cell proliferation, cytokine production, and generation of CTL.";
J. Immunol. 154:97-105(1995).
[11]
IDENTIFICATION AS CD86.
PubMed=7520767;
Engel P., Gribben J.G., Freeman G.J., Zhou L.J., Nozawa Y., Abe M.,
Nadler L.M., Wakasa H., Tedder T.F.;
"The B7-2 (B70) costimulatory molecule expressed by monocytes and
activated B lymphocytes is the CD86 differentiation antigen.";
Blood 84:1402-1407(1994).
[12]
UBIQUITINATION, AND INTERACTION WITH MARCH8.
PubMed=12582153; DOI=10.1074/jbc.M211285200;
Goto E., Ishido S., Sato Y., Ohgimoto S., Ohgimoto K.,
Nagano-Fujii M., Hotta H.;
"c-MIR, a human E3 ubiquitin ligase, is a functional homolog of
herpesvirus proteins MIR1 and MIR2 and has similar activity.";
J. Biol. Chem. 278:14657-14668(2003).
[13]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS
SUBGROUP B FIBER PROTEINS.
PubMed=16920215; DOI=10.1016/j.virusres.2006.07.009;
Short J.J., Vasu C., Holterman M.J., Curiel D.T., Pereboev A.;
"Members of adenovirus species B utilize CD80 and CD86 as cellular
attachment receptors.";
Virus Res. 122:144-153(2006).
[14]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-134 IN COMPLEX WITH CTLA4.
PubMed=11279501; DOI=10.1038/35069112;
Schwartz J.C., Zhang X., Fedorov A.A., Nathenson S.G., Almo S.C.;
"Structural basis for co-stimulation by the human CTLA-4/B7-2
complex.";
Nature 410:604-608(2001).
[15]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 26-134, SUBUNIT, AND
DISULFIDE BOND.
PubMed=12606712; DOI=10.1073/pnas.252771499;
Zhang X., Schwartz J.C., Almo S.C., Nathenson S.G.;
"Crystal structure of the receptor-binding domain of human B7-2:
insights into organization and signaling.";
Proc. Natl. Acad. Sci. U.S.A. 100:2586-2591(2003).
-!- FUNCTION: Receptor involved in the costimulatory signal essential
for T-lymphocyte proliferation and interleukin-2 production, by
binding CD28 or CTLA-4. May play a critical role in the early
events of T-cell activation and costimulation of naive T-cells,
such as deciding between immunity and anergy that is made by T-
cells within 24 hours after activation. Isoform 2 interferes with
the formation of CD86 clusters, and thus acts as a negative
regulator of T-cell activation.
-!- FUNCTION: (Microbial infection) Acts as a receptor for adenovirus
subgroup B. {ECO:0000269|PubMed:16920215}.
-!- SUBUNIT: Homodimer. Interacts with MARCH8.
{ECO:0000269|PubMed:11279501, ECO:0000269|PubMed:12582153,
ECO:0000269|PubMed:12606712, ECO:0000305}.
-!- SUBUNIT: (Microbial infection) Interacts with adenovirus subgroup
b fiber protein. {ECO:0000269|PubMed:16920215}.
-!- INTERACTION:
P16410:CTLA4; NbExp=3; IntAct=EBI-1030956, EBI-1030991;
P01552:entB (xeno); NbExp=5; IntAct=EBI-15945259, EBI-1027464;
Q99XW1:smeZ (xeno); NbExp=2; IntAct=EBI-15945259, EBI-16212640;
P06886:tst (xeno); NbExp=2; IntAct=EBI-15945259, EBI-16211350;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=P42081-1; Sequence=Displayed;
Name=2;
IsoId=P42081-3; Sequence=VSP_023124;
Name=3; Synonyms=CD86 deltaEC;
IsoId=P42081-2; Sequence=VSP_023124, VSP_009125;
Name=4; Synonyms=CD86 deltaTM;
IsoId=P42081-4; Sequence=VSP_023124, VSP_040324;
Name=5;
IsoId=P42081-5; Sequence=VSP_047221;
Note=No experimental confirmation available.;
Name=6;
IsoId=P42081-6; Sequence=VSP_047220;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed by activated B-lymphocytes and
monocytes.
-!- PTM: Polyubiquitinated; which is promoted by MARCH8 and results in
endocytosis and lysosomal degradation.
{ECO:0000269|PubMed:12582153}.
-!- WEB RESOURCE: Name=Wikipedia; Note=CD86 entry;
URL="https://en.wikipedia.org/wiki/CD86";
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EMBL; U04343; AAB03814.1; -; mRNA.
EMBL; L25259; AAA58389.1; -; mRNA.
EMBL; CR541844; CAG46642.1; -; mRNA.
EMBL; EF064748; ABK41931.1; -; Genomic_DNA.
EMBL; AK294663; BAH11839.1; -; mRNA.
EMBL; AK301237; BAH13438.1; -; mRNA.
EMBL; AK316203; BAH14574.1; -; mRNA.
EMBL; AC068630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC040261; AAH40261.1; -; mRNA.
EMBL; U17722; AAA86473.1; -; Genomic_DNA.
EMBL; U17717; AAA86473.1; JOINED; Genomic_DNA.
EMBL; U17718; AAA86473.1; JOINED; Genomic_DNA.
EMBL; U17719; AAA86473.1; JOINED; Genomic_DNA.
EMBL; U17721; AAA86473.1; JOINED; Genomic_DNA.
CCDS; CCDS3009.1; -. [P42081-1]
CCDS; CCDS43138.1; -. [P42081-3]
CCDS; CCDS56272.1; -. [P42081-5]
CCDS; CCDS56273.1; -. [P42081-6]
CCDS; CCDS74991.1; -. [P42081-4]
PIR; A48754; A48754.
PIR; JC7605; JC7605.
RefSeq; NP_001193853.1; NM_001206924.1.
RefSeq; NP_001193854.1; NM_001206925.1.
RefSeq; NP_008820.3; NM_006889.4.
RefSeq; NP_787058.4; NM_175862.4.
RefSeq; NP_795711.1; NM_176892.1.
UniGene; Hs.171182; -.
PDB; 1I85; X-ray; 3.20 A; A/B=26-134.
PDB; 1NCN; X-ray; 2.70 A; A/B=26-134.
PDBsum; 1I85; -.
PDBsum; 1NCN; -.
ProteinModelPortal; P42081; -.
SMR; P42081; -.
BioGrid; 107380; 6.
DIP; DIP-35606N; -.
IntAct; P42081; 8.
STRING; 9606.ENSP00000332049; -.
ChEMBL; CHEMBL2364156; -.
DrugBank; DB01281; Abatacept.
DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
DrugBank; DB06681; Belatacept.
GuidetoPHARMACOLOGY; 2745; -.
iPTMnet; P42081; -.
PhosphoSitePlus; P42081; -.
BioMuta; CD86; -.
DMDM; 317373339; -.
PaxDb; P42081; -.
PeptideAtlas; P42081; -.
PRIDE; P42081; -.
ProteomicsDB; 55481; -.
ProteomicsDB; 55482; -. [P42081-2]
ProteomicsDB; 55483; -. [P42081-3]
ProteomicsDB; 55484; -. [P42081-4]
DNASU; 942; -.
Ensembl; ENST00000264468; ENSP00000264468; ENSG00000114013. [P42081-4]
Ensembl; ENST00000330540; ENSP00000332049; ENSG00000114013. [P42081-1]
Ensembl; ENST00000393627; ENSP00000377248; ENSG00000114013. [P42081-3]
Ensembl; ENST00000469710; ENSP00000418988; ENSG00000114013. [P42081-6]
Ensembl; ENST00000493101; ENSP00000420230; ENSG00000114013. [P42081-5]
GeneID; 942; -.
KEGG; hsa:942; -.
UCSC; uc003eet.4; human. [P42081-1]
CTD; 942; -.
DisGeNET; 942; -.
EuPathDB; HostDB:ENSG00000114013.15; -.
GeneCards; CD86; -.
HGNC; HGNC:1705; CD86.
HPA; CAB004319; -.
MIM; 601020; gene.
neXtProt; NX_P42081; -.
OpenTargets; ENSG00000114013; -.
PharmGKB; PA26243; -.
eggNOG; ENOG410IYP1; Eukaryota.
eggNOG; ENOG410ZD66; LUCA.
GeneTree; ENSGT00720000108819; -.
HOGENOM; HOG000276893; -.
HOVERGEN; HBG004093; -.
InParanoid; P42081; -.
KO; K05413; -.
OMA; ELVVFWQ; -.
OrthoDB; EOG091G0QVY; -.
PhylomeDB; P42081; -.
TreeFam; TF331083; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-389356; CD28 co-stimulation.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SIGNOR; P42081; -.
ChiTaRS; CD86; human.
EvolutionaryTrace; P42081; -.
GeneWiki; CD86; -.
GenomeRNAi; 942; -.
PRO; PR:P42081; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114013; Expressed in 172 organ(s), highest expression level in leukocyte.
CleanEx; HS_CD86; -.
ExpressionAtlas; P42081; baseline and differential.
Genevisible; P42081; HS.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015026; F:coreceptor activity; NAS:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; NAS:UniProtKB.
GO; GO:0045404; P:positive regulation of interleukin-4 biosynthetic process; NAS:UniProtKB.
GO; GO:0043017; P:positive regulation of lymphotoxin A biosynthetic process; NAS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; NAS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
CDD; cd16087; IgV_CD86; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR037677; CD86_IgV.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF13895; Ig_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Immunity;
Immunoglobulin domain; Membrane; Polymorphism; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Ubl conjugation.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 329 T-lymphocyte activation antigen CD86.
/FTId=PRO_0000014550.
TOPO_DOM 24 247 Extracellular. {ECO:0000255}.
TRANSMEM 248 268 Helical. {ECO:0000255}.
TOPO_DOM 269 329 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 131 Ig-like V-type.
DOMAIN 150 225 Ig-like C2-type.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 40 110 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:12606712}.
DISULFID 157 218 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 82 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_047220.
VAR_SEQ 1 6 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:11162656,
ECO:0000303|PubMed:7694153,
ECO:0000303|Ref.4}.
/FTId=VSP_023124.
VAR_SEQ 22 234 Missing (in isoform 3).
{ECO:0000303|PubMed:11162656}.
/FTId=VSP_009125.
VAR_SEQ 22 133 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047221.
VAR_SEQ 235 282 Missing (in isoform 4).
{ECO:0000303|PubMed:11162656}.
/FTId=VSP_040324.
VARIANT 170 170 S -> N (in dbSNP:rs9282642).
/FTId=VAR_021916.
VARIANT 185 185 V -> I (in dbSNP:rs2681417).
{ECO:0000269|PubMed:11162656,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7541777,
ECO:0000269|PubMed:7694153,
ECO:0000269|PubMed:7694363,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_055003.
VARIANT 310 310 A -> T (in dbSNP:rs1129055).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_014650.
VARIANT 323 323 D -> N (in dbSNP:rs9282648).
/FTId=VAR_021917.
CONFLICT 27 27 K -> E (in Ref. 9; AAA86473).
{ECO:0000305}.
STRAND 26 31 {ECO:0000244|PDB:1NCN}.
STRAND 36 39 {ECO:0000244|PDB:1NCN}.
HELIX 50 52 {ECO:0000244|PDB:1NCN}.
STRAND 53 59 {ECO:0000244|PDB:1NCN}.
STRAND 64 69 {ECO:0000244|PDB:1NCN}.
STRAND 76 78 {ECO:0000244|PDB:1NCN}.
TURN 80 84 {ECO:0000244|PDB:1NCN}.
STRAND 85 89 {ECO:0000244|PDB:1NCN}.
TURN 90 93 {ECO:0000244|PDB:1NCN}.
STRAND 94 97 {ECO:0000244|PDB:1NCN}.
HELIX 102 104 {ECO:0000244|PDB:1NCN}.
STRAND 106 115 {ECO:0000244|PDB:1NCN}.
STRAND 117 133 {ECO:0000244|PDB:1NCN}.
SEQUENCE 329 AA; 37682 MW; C249DAEEB889D911 CRC64;
MDPQCTMGLS NILFVMAFLL SGAAPLKIQA YFNETADLPC QFANSQNQSL SELVVFWQDQ
ENLVLNEVYL GKEKFDSVHS KYMGRTSFDS DSWTLRLHNL QIKDKGLYQC IIHHKKPTGM
IRIHQMNSEL SVLANFSQPE IVPISNITEN VYINLTCSSI HGYPEPKKMS VLLRTKNSTI
EYDGVMQKSQ DNVTELYDVS ISLSVSFPDV TSNMTIFCIL ETDKTRLLSS PFSIELEDPQ
PPPDHIPWIT AVLPTVIICV MVFCLILWKW KKKKRPRNSY KCGTNTMERE ESEQTKKREK
IHIPERSDEA QRVFKSSKTS SCDKSDTCF


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