CD27_HUMAN
ID CD27_HUMAN Reviewed; 260 AA.
AC P26842; B2RDZ0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=CD27 antigen;
DE AltName: Full=CD27L receptor;
DE AltName: Full=T-cell activation antigen CD27;
DE AltName: Full=T14;
DE AltName: Full=Tumor necrosis factor receptor superfamily member 7;
DE AltName: CD_antigen=CD27;
DE Flags: Precursor;
GN Name=CD27; Synonyms=TNFRSF7;
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], AND VARIANT ARG-233.
RC TISSUE=Monocyte;
RX PubMed=1655907;
RA Camerini D., Walz G., Loenen W.A.M., Borst J., Seed B.;
RT "The T cell activation antigen CD27 is a member of the nerve growth
RT factor/tumor necrosis factor receptor gene family.";
RL J. Immunol. 147:3165-3169(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-59 AND ARG-233.
RX PubMed=1334106;
RA Loenen W.A., Gravestein L.A., Beumer S., Melief C.J., Hagemeijer A.,
RA Borst J.;
RT "Genomic organization and chromosomal localization of the human CD27
RT gene.";
RL J. Immunol. 149:3937-3943(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-59 AND ARG-233.
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-59 AND ARG-233.
RG NIEHS SNPs program;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-233.
RC TISSUE=B-cell;
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 PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP INTERACTION WITH TRAF2.
RX PubMed=9692890;
RX DOI=10.1002/(sici)1521-4141(199807)28:07<2208::aid-immu2208>3.0.co;2-l;
RA Gravestein L.A., Amsen D., Boes M., Calvo C.R., Kruisbeek A.M., Borst J.;
RT "The TNF receptor family member CD27 signals to Jun N-terminal kinase via
RT Traf-2.";
RL Eur. J. Immunol. 28:2208-2216(1998).
RN [9]
RP INTERACTION WITH SIVA1.
RC TISSUE=Cervix carcinoma, and Thymus;
RX PubMed=9177220; DOI=10.1073/pnas.94.12.6346;
RA Prasad K.V.S., Ao Z., Yoon Y., Wu M.X., Rizk M., Jacquot S.,
RA Schlossman S.F.;
RT "CD27, a member of the tumor necrosis factor receptor family, induces
RT apoptosis and binds to Siva, a proapoptotic protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6346-6351(1997).
RN [10]
RP GLYCOSYLATION AT SER-127, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [11]
RP INVOLVEMENT IN LPFS2.
RX PubMed=22197273; DOI=10.1016/j.jaci.2011.11.013;
RA van Montfrans J.M., Hoepelman A.I., Otto S., van Gijn M., van de Corput L.,
RA de Weger R.A., Monaco-Shawver L., Banerjee P.P., Sanders E.A.,
RA Jol-van der Zijde C.M., Betts M.R., Orange J.S., Bloem A.C., Tesselaar K.;
RT "CD27 deficiency is associated with combined immunodeficiency and
RT persistent symptomatic EBV viremia.";
RL J. Allergy Clin. Immunol. 129:787-793(2012).
RN [12]
RP VARIANT LPFS2 TYR-53.
RX PubMed=22801960; DOI=10.3324/haematol.2012.068791;
RA Salzer E., Daschkey S., Choo S., Gombert M., Santos-Valente E., Ginzel S.,
RA Schwendinger M., Haas O.A., Fritsch G., Pickl W.F., Foerster-Waldl E.,
RA Borkhardt A., Boztug K., Bienemann K., Seidel M.G.;
RT "Combined immunodeficiency with life-threatening EBV-associated
RT lymphoproliferative disorder in patients lacking functional CD27.";
RL Haematologica 98:473-478(2013).
CC -!- FUNCTION: Receptor for CD70/CD27L. May play a role in survival of
CC activated T-cells. May play a role in apoptosis through association
CC with SIVA1.
CC -!- SUBUNIT: Homodimer. Interacts with SIVA1 and TRAF2.
CC {ECO:0000269|PubMed:9177220, ECO:0000269|PubMed:9692890}.
CC -!- INTERACTION:
CC P26842; P35609: ACTN2; NbExp=3; IntAct=EBI-520729, EBI-77797;
CC P26842; Q99828: CIB1; NbExp=7; IntAct=EBI-520729, EBI-372594;
CC P26842; O15304: SIVA1; NbExp=3; IntAct=EBI-520729, EBI-520756;
CC P26842; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-520729, EBI-5235340;
CC P26842; PRO_0000449624 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-520729, EBI-25475868;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Found in most T-lymphocytes.
CC -!- PTM: Phosphorylated.
CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans.
CC {ECO:0000269|PubMed:22171320}.
CC -!- DISEASE: Lymphoproliferative syndrome 2 (LPFS2) [MIM:615122]: An
CC autosomal recessive immunodeficiency disorder associated with
CC persistent symptomatic EBV viremia, hypogammaglobulinemia, and impaired
CC T-cell-dependent B-cell responses and T-cell dysfunction. The phenotype
CC is highly variable, ranging from asymptomatic borderline-low
CC hypogammaglobulinemia, to a full-blown symptomatic systemic
CC inflammatory response with life-threatening EBV-related complications,
CC including hemophagocytic lymphohistiocytosis, a lymphoproliferative
CC disorder, and malignant lymphoma requiring stem cell transplantation.
CC {ECO:0000269|PubMed:22197273, ECO:0000269|PubMed:22801960}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tnfrsf7/";
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DR EMBL; M63928; AAA58411.1; -; mRNA.
DR EMBL; AK315732; BAG38087.1; -; mRNA.
DR EMBL; AY504961; AAR84239.1; -; Genomic_DNA.
DR EMBL; AC005840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012160; AAH12160.1; -; mRNA.
DR CCDS; CCDS8545.1; -.
DR PIR; A46517; A46517.
DR RefSeq; NP_001233.1; NM_001242.4.
DR PDB; 5TL5; X-ray; 1.80 A; A=21-121.
DR PDB; 5TLJ; X-ray; 3.50 A; X=21-121.
DR PDB; 5TLK; X-ray; 2.70 A; X/Y=21-121.
DR PDB; 7KX0; X-ray; 2.69 A; D/E/F=23-127.
DR PDBsum; 5TL5; -.
DR PDBsum; 5TLJ; -.
DR PDBsum; 5TLK; -.
DR PDBsum; 7KX0; -.
DR AlphaFoldDB; P26842; -.
DR SMR; P26842; -.
DR BioGRID; 107377; 76.
DR ELM; P26842; -.
DR IntAct; P26842; 28.
DR STRING; 9606.ENSP00000266557; -.
DR ChEMBL; CHEMBL3713333; -.
DR GlyConnect; 800; 3 N-Linked glycans (1 site), 1 O-Linked glycan (1 site).
DR GlyGen; P26842; 4 sites, 3 N-linked glycans (1 site), 2 O-linked glycans (3 sites).
DR iPTMnet; P26842; -.
DR PhosphoSitePlus; P26842; -.
DR SwissPalm; P26842; -.
DR BioMuta; CD27; -.
DR DMDM; 269849546; -.
DR EPD; P26842; -.
DR jPOST; P26842; -.
DR MassIVE; P26842; -.
DR PaxDb; P26842; -.
DR PeptideAtlas; P26842; -.
DR PRIDE; P26842; -.
DR ProteomicsDB; 54366; -.
DR ABCD; P26842; 16 sequenced antibodies.
DR Antibodypedia; 3716; 2002 antibodies from 50 providers.
DR CPTC; P26842; 3 antibodies.
DR DNASU; 939; -.
DR Ensembl; ENST00000266557.4; ENSP00000266557.3; ENSG00000139193.4.
DR GeneID; 939; -.
DR KEGG; hsa:939; -.
DR MANE-Select; ENST00000266557.4; ENSP00000266557.3; NM_001242.5; NP_001233.2.
DR UCSC; uc001qod.4; human.
DR CTD; 939; -.
DR DisGeNET; 939; -.
DR GeneCards; CD27; -.
DR HGNC; HGNC:11922; CD27.
DR HPA; ENSG00000139193; Tissue enriched (lymphoid).
DR MalaCards; CD27; -.
DR MIM; 186711; gene.
DR MIM; 615122; phenotype.
DR neXtProt; NX_P26842; -.
DR OpenTargets; ENSG00000139193; -.
DR Orphanet; 238505; Combined immunodeficiency due to CD27 deficiency.
DR PharmGKB; PA162382107; -.
DR VEuPathDB; HostDB:ENSG00000139193; -.
DR eggNOG; ENOG502SBE3; Eukaryota.
DR GeneTree; ENSGT00510000049297; -.
DR HOGENOM; CLU_067121_0_0_1; -.
DR InParanoid; P26842; -.
DR OMA; HGEAAQC; -.
DR OrthoDB; 577429at2759; -.
DR PhylomeDB; P26842; -.
DR TreeFam; TF336960; -.
DR PathwayCommons; P26842; -.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; P26842; -.
DR SIGNOR; P26842; -.
DR BioGRID-ORCS; 939; 15 hits in 1068 CRISPR screens.
DR GeneWiki; CD27; -.
DR GenomeRNAi; 939; -.
DR Pharos; P26842; Tbio.
DR PRO; PR:P26842; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P26842; protein.
DR Bgee; ENSG00000139193; Expressed in lymph node and 97 other tissues.
DR Genevisible; P26842; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; NAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; NAS:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; NAS:UniProtKB.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:InterPro.
DR CDD; cd13408; TNFRSF7; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR022328; TNFR_7.
DR InterPro; IPR034000; TNFRSF7_N.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01960; TNFACTORR7.
DR SMART; SM00208; TNFR; 2.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 20..260
FT /note="CD27 antigen"
FT /id="PRO_0000034571"
FT TOPO_DOM 20..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 26..63
FT /note="TNFR-Cys 1"
FT REPEAT 64..104
FT /note="TNFR-Cys 2"
FT REPEAT 105..141
FT /note="TNFR-Cys 3"
FT REGION 219..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:22171320"
FT DISULFID 27..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 40..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 43..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 65..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 84..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 87..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 106..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 112..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VARIANT 53
FT /note="C -> Y (in LPFS2; dbSNP:rs397514667)"
FT /evidence="ECO:0000269|PubMed:22801960"
FT /id="VAR_069793"
FT VARIANT 59
FT /note="A -> T (in dbSNP:rs25680)"
FT /evidence="ECO:0000269|PubMed:1334106,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_016148"
FT VARIANT 233
FT /note="H -> R (in dbSNP:rs2532502)"
FT /evidence="ECO:0000269|PubMed:1334106,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:1655907, ECO:0000269|Ref.4"
FT /id="VAR_052348"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5TL5"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:5TL5"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:5TL5"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5TL5"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:5TL5"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:5TL5"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5TL5"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:5TL5"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:7KX0"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5TL5"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5TL5"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5TL5"
SQ SEQUENCE 260 AA; 29137 MW; 43C38B895B2AD4E2 CRC64;
MARPHPWWLC VLGTLVGLSA TPAPKSCPER HYWAQGKLCC QMCEPGTFLV KDCDQHRKAA
QCDPCIPGVS FSPDHHTRPH CESCRHCNSG LLVRNCTITA NAECACRNGW QCRDKECTEC
DPLPNPSLTA RSSQALSPHP QPTHLPYVSE MLEARTAGHM QTLADFRQLP ARTLSTHWPP
QRSLCSSDFI RILVIFSGMF LVFTLAGALF LHQRRKYRSN KGESPVEPAE PCHYSCPREE
EGSTIPIQED YRKPEPACSP
