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   27-MAR-2024, entry version 212.
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   PDB; 8DS5; X-ray; 1.93 A; A=21-177.
DR   PDBsum; 5TL5; -.
DR   PDBsum; 5TLJ; -.
DR   PDBsum; 5TLK; -.
DR   PDBsum; 7KX0; -.
DR   PDBsum; 8DS5; -.
DR   AlphaFoldDB; P26842; -.
DR   SMR; P26842; -.
DR   BioGRID; 107377; 77.
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   GlyCosmos; P26842; 4 sites, 5 glycans.
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; 9606-ENSP00000266557; -.
DR   PeptideAtlas; P26842; -.
DR   ProteomicsDB; 54366; -.
DR   ABCD; P26842; 16 sequenced antibodies.
DR   Antibodypedia; 3716; 2442 antibodies from 51 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   AGR; HGNC:11922; -.
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; LSTHWSP; -.
DR   OrthoDB; 4711092at2759; -.
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; 20 hits in 1149 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 cell types or tissues.
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: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 non-canonical NF-kappaB signal transduction; NAS:UniProtKB.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:InterPro.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   CDD; cd13408; TNFRSF7; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR022328; TNFR_7.
DR   InterPro; IPR034000; TNFRSF7_N.
DR   PANTHER; PTHR47496; CD27; 1.
DR   PANTHER; PTHR47496:SF1; CD27 ANTIGEN; 1.
DR   Pfam; PF00020; TNFR_c6; 1.
DR   PRINTS; PR01960; TNFACTORR7.
DR   SMART; SM00208; TNFR; 2.
DR   SUPFAM; SSF57586; TNF receptor-like; 2.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 1.
DR   Genevisible; P26842; HS.
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
//