CD8B_HUMAN
ID CD8B_HUMAN Reviewed; 210 AA.
AC P10966; P14860; P14861; Q15980; Q496E0; Q496E1; Q496E2; Q9UDB4; Q9UDB5;
AC Q9UDB6; Q9UDB7; Q9UDB8; Q9UDB9; Q9UDC0; Q9UQ55;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=T-cell surface glycoprotein CD8 beta chain;
DE AltName: CD_antigen=CD8b;
DE Flags: Precursor;
GN Name=CD8B; Synonyms=CD8B1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=T-cell;
RX PubMed=3145195; DOI=10.1002/j.1460-2075.1988.tb03217.x;
RA Norment A.M., Littman D.R.;
RT "A second subunit of CD8 is expressed in human T cells.";
RL EMBO J. 7:3433-3439(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CD8A, AND
RP SUBCELLULAR LOCATION.
RX PubMed=3145196; DOI=10.1002/j.1460-2075.1988.tb03221.x;
RA Disanto J.P., Knowles R.W., Flomenberg N.;
RT "The human Lyt-3 molecule requires CD8 for cell surface expression.";
RL EMBO J. 7:3465-3470(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3264320; DOI=10.1084/jem.168.6.1993;
RA Shiue L., Gorman S.D., Parnes J.R.;
RT "A second chain of human CD8 is expressed on peripheral blood
RT lymphocytes.";
RL J. Exp. Med. 168:1993-2005(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=1541829;
RA Nakayama K., Kawachi Y., Tokito S., Minami N., Yamamoto R., Imai T.,
RA Gachelin G., Nakauchi H.;
RT "Recent duplication of the two human CD8 beta-chain genes.";
RL J. Immunol. 148:1919-1927(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-210 (ISOFORMS 1; 2; 3; 5; 6; 7 AND 8),
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood;
RX PubMed=8436166; DOI=10.1002/eji.1830230203;
RA DiSanto J.P., Smith D., de Bruin D., Lacy E., Flomenberg N.;
RT "Transcriptional diversity at the duplicated human CD8 beta loci.";
RL Eur. J. Immunol. 23:320-326(1993).
RN [8]
RP FUNCTION, PALMITOYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH LCK.
RX PubMed=10925291; DOI=10.4049/jimmunol.165.4.2068;
RA Arcaro A., Gregoire C., Boucheron N., Stotz S., Palmer E., Malissen B.,
RA Luescher I.F.;
RT "Essential role of CD8 palmitoylation in CD8 coreceptor function.";
RL J. Immunol. 165:2068-2076(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LCK.
RX PubMed=11714755; DOI=10.1084/jem.194.10.1485;
RA Arcaro A., Gregoire C., Bakker T.R., Baldi L., Jordan M., Goffin L.,
RA Boucheron N., Wurm F., van der Merwe P.A., Malissen B., Luescher I.F.;
RT "CD8beta endows CD8 with efficient coreceptor function by coupling T cell
RT receptor/CD3 to raft-associated CD8/p56(lck) complexes.";
RL J. Exp. Med. 194:1485-1495(2001).
RN [10]
RP FUNCTION.
RX PubMed=17145893; DOI=10.1158/0008-5472.can-06-2379;
RA Lyons G.E., Moore T., Brasic N., Li M., Roszkowski J.J., Nishimura M.I.;
RT "Influence of human CD8 on antigen recognition by T-cell receptor-
RT transduced cells.";
RL Cancer Res. 66:11455-11461(2006).
CC -!- FUNCTION: Integral membrane glycoprotein that plays an essential role
CC in the immune response and serves multiple functions in responses
CC against both external and internal offenses. In T-cells, functions
CC primarily as a coreceptor for MHC class I molecule:peptide complex. The
CC antigens presented by class I peptides are derived from cytosolic
CC proteins while class II derived from extracellular proteins. Interacts
CC simultaneously with the T-cell receptor (TCR) and the MHC class I
CC proteins presented by antigen presenting cells (APCs). In turn,
CC recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. A
CC palmitoylation site in the cytoplasmic tail of CD8B chain contributes
CC to partitioning of CD8 into the plasma membrane lipid rafts where
CC signaling proteins are enriched. Once LCK recruited, it initiates
CC different intracellular signaling pathways by phosphorylating various
CC substrates ultimately leading to lymphokine production, motility,
CC adhesion and activation of cytotoxic T-lymphocytes (CTLs).
CC Additionally, plays a critical role in thymic selection of CD8+ T-
CC cells. {ECO:0000250|UniProtKB:P10300, ECO:0000269|PubMed:10925291,
CC ECO:0000269|PubMed:11714755, ECO:0000269|PubMed:17145893}.
CC -!- SUBUNIT: Forms disulfide-linked heterodimers with CD8A at the cell
CC surface. Interacts with CD3D; this interaction couples TCR-CD3 with
CC CD8. Interacts with LCK. {ECO:0000250|UniProtKB:P10300,
CC ECO:0000269|PubMed:10925291, ECO:0000269|PubMed:11714755}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:11714755, ECO:0000269|PubMed:3145196}; Single-pass
CC type I membrane protein {ECO:0000305}. Note=Requires the partner CD8A
CC for efficient cell surface expression (PubMed:3145196). The heterodimer
CC CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic tail
CC palmitoylation. {ECO:0000269|PubMed:10925291,
CC ECO:0000269|PubMed:11714755, ECO:0000269|PubMed:3145196}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=M-1, Mbeta1;
CC IsoId=P10966-1; Sequence=Displayed;
CC Name=2; Synonyms=M-3, Mbeta2;
CC IsoId=P10966-2; Sequence=VSP_002490;
CC Name=3; Synonyms=S-1, Sbeta3;
CC IsoId=P10966-3; Sequence=VSP_002492, VSP_002493;
CC Name=4; Synonyms=M-2;
CC IsoId=P10966-4; Sequence=VSP_002491;
CC Name=5; Synonyms=Mbeta3;
CC IsoId=P10966-6; Sequence=VSP_002493;
CC Name=6; Synonyms=Sbeta1;
CC IsoId=P10966-7; Sequence=VSP_002492;
CC Name=7; Synonyms=Sbeta4;
CC IsoId=P10966-8; Sequence=VSP_039654;
CC Name=8; Synonyms=Sbeta5;
CC IsoId=P10966-9; Sequence=VSP_039655;
CC -!- TISSUE SPECIFICITY: Isoform 1, isoform 3, isoform 5, isoform 6, isoform
CC 7 and isoform 8 are expressed in both thymus and peripheral CD8+ T-
CC cells. Expression of isoform 1 is higher in thymus CD8+ T-cells than in
CC peripheral CD8+ T-cells. Expression of isoform 6 is higher in
CC peripheral CD8+ T-cells than in thymus CD8+ T-cells.
CC {ECO:0000269|PubMed:8436166}.
CC -!- PTM: Phosphorylated as a consequence of T-cell activation.
CC {ECO:0000305}.
CC -!- PTM: Palmitoylated at the cytoplasmic tail and thereby targets the
CC heterodimer CD8A/CD8B to lipid rafts unlike CD8A homodimers.
CC {ECO:0000269|PubMed:10925291}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD13877.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD8 entry;
CC URL="https://en.wikipedia.org/wiki/CD8";
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DR EMBL; X13444; CAA31795.1; -; mRNA.
DR EMBL; X13445; CAA31796.1; -; mRNA.
DR EMBL; X13446; CAA31797.1; -; mRNA.
DR EMBL; X13452; CAA31803.1; -; mRNA.
DR EMBL; Y00805; CAA68750.1; -; mRNA.
DR EMBL; M36712; AAA35664.1; -; mRNA.
DR EMBL; S87090; AAB21669.2; -; Genomic_DNA.
DR EMBL; S87068; AAB21669.2; JOINED; Genomic_DNA.
DR EMBL; S87070; AAB21669.2; JOINED; Genomic_DNA.
DR EMBL; S87073; AAB21669.2; JOINED; Genomic_DNA.
DR EMBL; S87081; AAB21669.2; JOINED; Genomic_DNA.
DR EMBL; S87087; AAB21670.2; -; Genomic_DNA.
DR EMBL; S87068; AAB21670.2; JOINED; Genomic_DNA.
DR EMBL; S87070; AAB21670.2; JOINED; Genomic_DNA.
DR EMBL; S87073; AAB21670.2; JOINED; Genomic_DNA.
DR EMBL; S87078; AAB21670.2; JOINED; Genomic_DNA.
DR EMBL; S87081; AAB21670.2; JOINED; Genomic_DNA.
DR EMBL; S87083; AAB21671.2; -; Genomic_DNA.
DR EMBL; S87068; AAB21671.2; JOINED; Genomic_DNA.
DR EMBL; S87070; AAB21671.2; JOINED; Genomic_DNA.
DR EMBL; S87073; AAB21671.2; JOINED; Genomic_DNA.
DR EMBL; S87078; AAB21671.2; JOINED; Genomic_DNA.
DR EMBL; S87081; AAB21671.2; JOINED; Genomic_DNA.
DR EMBL; S87083; AAB21672.2; -; Genomic_DNA.
DR EMBL; S87068; AAB21672.2; JOINED; Genomic_DNA.
DR EMBL; S87070; AAB21672.2; JOINED; Genomic_DNA.
DR EMBL; S87073; AAB21672.2; JOINED; Genomic_DNA.
DR EMBL; S87078; AAB21672.2; JOINED; Genomic_DNA.
DR EMBL; S87081; AAB21672.2; JOINED; Genomic_DNA.
DR EMBL; AC111200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100911; AAI00912.1; -; mRNA.
DR EMBL; BC100912; AAI00913.1; -; mRNA.
DR EMBL; BC100913; AAI00914.1; -; mRNA.
DR EMBL; BC100914; AAI00915.1; -; mRNA.
DR EMBL; S55731; AAD13877.1; ALT_SEQ; Genomic_DNA.
DR EMBL; S55730; AAD13877.1; JOINED; Genomic_DNA.
DR EMBL; S55733; AAD13877.1; JOINED; Genomic_DNA.
DR CCDS; CCDS1994.1; -. [P10966-3]
DR CCDS; CCDS1995.1; -. [P10966-6]
DR CCDS; CCDS1997.1; -. [P10966-1]
DR CCDS; CCDS42708.1; -. [P10966-2]
DR CCDS; CCDS54376.1; -. [P10966-9]
DR PIR; C49050; C49050.
DR PIR; D46482; D46482.
DR PIR; E49050; E49050.
DR PIR; G49050; G49050.
DR PIR; S01647; E46482.
DR PIR; S01873; C46482.
DR PIR; S01874; B46482.
DR PIR; T01073; T01073.
DR RefSeq; NP_001171571.1; NM_001178100.1. [P10966-9]
DR RefSeq; NP_004922.1; NM_004931.4. [P10966-1]
DR RefSeq; NP_742099.1; NM_172101.3. [P10966-2]
DR RefSeq; NP_742100.1; NM_172102.3. [P10966-3]
DR RefSeq; NP_757362.1; NM_172213.3. [P10966-6]
DR AlphaFoldDB; P10966; -.
DR SMR; P10966; -.
DR BioGRID; 107364; 18.
DR ComplexPortal; CPX-6741; CD8alpha-beta complex.
DR GlyGen; P10966; 1 site.
DR iPTMnet; P10966; -.
DR PhosphoSitePlus; P10966; -.
DR SwissPalm; P10966; -.
DR BioMuta; CD8B; -.
DR DMDM; 116032; -.
DR MassIVE; P10966; -.
DR PaxDb; P10966; -.
DR PeptideAtlas; P10966; -.
DR PRIDE; P10966; -.
DR ProteomicsDB; 52679; -. [P10966-1]
DR ProteomicsDB; 52680; -. [P10966-2]
DR ProteomicsDB; 52681; -. [P10966-3]
DR ProteomicsDB; 52682; -. [P10966-4]
DR ProteomicsDB; 52683; -. [P10966-6]
DR ProteomicsDB; 52684; -. [P10966-7]
DR ProteomicsDB; 52685; -. [P10966-8]
DR ProteomicsDB; 52686; -. [P10966-9]
DR ProteomicsDB; 61988; -.
DR Antibodypedia; 3816; 1105 antibodies from 40 providers.
DR DNASU; 926; -.
DR Ensembl; ENST00000331469.6; ENSP00000331172.2; ENSG00000172116.23. [P10966-6]
DR Ensembl; ENST00000349455.7; ENSP00000340592.3; ENSG00000172116.23. [P10966-3]
DR Ensembl; ENST00000390655.12; ENSP00000375070.6; ENSG00000172116.23. [P10966-1]
DR Ensembl; ENST00000393759.6; ENSP00000377356.2; ENSG00000172116.23. [P10966-2]
DR Ensembl; ENST00000393761.6; ENSP00000377358.2; ENSG00000172116.23. [P10966-9]
DR GeneID; 926; -.
DR KEGG; hsa:926; -.
DR MANE-Select; ENST00000390655.12; ENSP00000375070.6; NM_004931.5; NP_004922.1.
DR UCSC; uc002srw.4; human. [P10966-1]
DR CTD; 926; -.
DR DisGeNET; 926; -.
DR GeneCards; CD8B; -.
DR HGNC; HGNC:1707; CD8B.
DR HPA; ENSG00000172116; Tissue enriched (lymphoid).
DR MIM; 186730; gene.
DR neXtProt; NX_P10966; -.
DR OpenTargets; ENSG00000172116; -.
DR PharmGKB; PA26245; -.
DR VEuPathDB; HostDB:ENSG00000172116; -.
DR eggNOG; ENOG502SANQ; Eukaryota.
DR GeneTree; ENSGT00510000048998; -.
DR HOGENOM; CLU_089344_0_0_1; -.
DR InParanoid; P10966; -.
DR OMA; RLWLRIH; -.
DR PhylomeDB; P10966; -.
DR TreeFam; TF338028; -.
DR PathwayCommons; P10966; -.
DR Reactome; R-HSA-182218; Nef Mediated CD8 Down-regulation.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 926; 43 hits in 1027 CRISPR screens.
DR GenomeRNAi; 926; -.
DR Pharos; P10966; Tbio.
DR PRO; PR:P10966; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P10966; protein.
DR Bgee; ENSG00000172116; Expressed in granulocyte and 98 other tissues.
DR ExpressionAtlas; P10966; baseline and differential.
DR Genevisible; P10966; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042101; C:T cell receptor complex; NAS:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; NAS:UniProtKB.
DR GO; GO:0042288; F:MHC class I protein binding; NAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IDA:ComplexPortal.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR042414; CD8B.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR11292; PTHR11292; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..210
FT /note="T-cell surface glycoprotein CD8 beta chain"
FT /id="PRO_0000014643"
FT TOPO_DOM 22..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..132
FT /note="Ig-like V-type"
FT MOD_RES 209
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 165..210
FT /note="GPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRRARLRFMKQFYK -> DF
FT TNKQRIGFWCPATKRHRSVMSTMWKNERRDTFNPGEFNGC (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:8436166"
FT /id="VSP_039654"
FT VAR_SEQ 166..210
FT /note="PLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRRARLRFMKQFYK -> LKG
FT KVYQEPLSPNACMDTTAILQPHRSCLTHGS (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8436166"
FT /id="VSP_039655"
FT VAR_SEQ 166..195
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:3145195,
FT ECO:0000303|PubMed:8436166"
FT /id="VSP_002492"
FT VAR_SEQ 208..210
FT /note="FYK -> LRLHPLEKCSRMDY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3145195,
FT ECO:0000303|PubMed:8436166"
FT /id="VSP_002490"
FT VAR_SEQ 208..210
FT /note="FYK -> PQGEGISGTFVPQCLHGYYSNTTTSQKLLNPWILKT (in
FT isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3145195, ECO:0000303|PubMed:8436166"
FT /id="VSP_002493"
FT VAR_SEQ 208..210
FT /note="FYK -> KFNIVCLKISGFTTCCCFQILQISREYGFGVLLQKDIGQ (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_002491"
FT CONFLICT 173
FT /note="Missing (in Ref. 7; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="V -> I (in Ref. 6; AAI00915)"
FT /evidence="ECO:0000305"
FT CONFLICT P10966-6:213
FT /note="I -> V (in Ref. 6; AAI00915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 23722 MW; 675AD919585F4B80 CRC64;
MRPRLWLLLA AQLTVLHGNS VLQQTPAYIK VQTNKMVMLS CEAKISLSNM RIYWLRQRQA
PSSDSHHEFL ALWDSAKGTI HGEEVEQEKI AVFRDASRFI LNLTSVKPED SGIYFCMIVG
SPELTFGKGT QLSVVDFLPT TAQPTKKSTL KKRVCRLPRP ETQKGPLCSP ITLGLLVAGV
LVLLVSLGVA IHLCCRRRRA RLRFMKQFYK
