TNF10_HUMAN
ID TNF10_HUMAN Reviewed; 281 AA.
AC P50591; A1Y9B3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 10;
DE AltName: Full=Apo-2 ligand;
DE Short=Apo-2L;
DE AltName: Full=TNF-related apoptosis-inducing ligand;
DE Short=Protein TRAIL;
DE AltName: CD_antigen=CD253;
GN Name=TNFSF10; Synonyms=APO2L, TRAIL;
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] (ISOFORM 1).
RX PubMed=8777713; DOI=10.1016/1074-7613(95)90057-8;
RA Wiley S.R., Schooley K., Smolak P.J., Din W.S., Huang C.-P., Nicholl J.K.,
RA Sutherland G.R., Davis-Smith T., Rauch C., Smith C.A., Goodwin R.G.;
RT "Identification and characterization of a new member of the TNF family that
RT induces apoptosis.";
RL Immunity 3:673-682(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8663110; DOI=10.1074/jbc.271.22.12687;
RA Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A.,
RA Ashkenazi A.;
RT "Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis
RT factor cytokine family.";
RL J. Biol. Chem. 271:12687-12690(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=21859711; DOI=10.1074/jbc.m111.274639;
RA Schnepple D.J., Shepard B., Bren G.D., Cummins N.W., Natesampillai S.,
RA Trushin S., Algeciras-Schimnich A., Meng X.W., Sainski A.M., Rizza S.A.,
RA Kaufmann S.H., Badley A.D.;
RT "Isolation of a TRAIL antagonist from the serum of HIV-infected patients.";
RL J. Biol. Chem. 286:35742-35754(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Woods D.C., Haugen M.J., Johnson A.L.;
RT "Novel TRAIL splice variant TRAIL-delta.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=14609566; DOI=10.1016/s1043-4666(03)00094-2;
RA Ehrlich S., Infante-Duarte C., Seeger B., Zipp F.;
RT "Regulation of soluble and surface-bound TRAIL in human T cells, B cells,
RT and monocytes.";
RL Cytokine 24:244-253(2003).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
RA Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
RA Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M.,
RA Dixon J.E., Yeo C.Y., Whitman M.;
RT "A secreted tyrosine kinase acts in the extracellular environment.";
RL Cell 158:1033-1044(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 114-281 IN COMPLEX WITH TNFRSF10B,
RP AND ZINC-BINDING SITE.
RX PubMed=10549288; DOI=10.1016/s1097-2765(00)80207-5;
RA Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M.,
RA Kelley R.F., Ashkenazi A., de Vos A.M.;
RT "Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex
RT with death receptor 5.";
RL Mol. Cell 4:563-571(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 119-281 IN COMPLEX WITH TNFRSF10B.
RX PubMed=10542098; DOI=10.1038/14935;
RA Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., Jones E.Y.,
RA Screaton G.R.;
RT "Structure of the TRAIL-DR5 complex reveals mechanisms conferring
RT specificity in apoptotic initiation.";
RL Nat. Struct. Biol. 6:1048-1053(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 114-281.
RX PubMed=10485660; DOI=10.1016/s1074-7613(00)80100-4;
RA Cha S.-S., Kim M.S., Choi Y.H., Sung B.J., Shin N.K., Shin H.C., Sung Y.C.,
RA Oh B.-H.;
RT "2.8 A resolution crystal structure of human TRAIL, a cytokine with
RT selective antitumor activity.";
RL Immunity 11:253-261(1999).
RN [13] {ECO:0007744|PDB:5CIR}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 114-281 IN COMPLEX WITH
RP TNFRSF10A, SUBUNIT, FUNCTION, AND ZINC-BINDING SITE.
RX PubMed=26457518; DOI=10.1107/s2053230x15016416;
RA Ramamurthy V., Yamniuk A.P., Lawrence E.J., Yong W., Schneeweis L.A.,
RA Cheng L., Murdock M., Corbett M.J., Doyle M.L., Sheriff S.;
RT "The structure of the death receptor 4-TNF-related apoptosis-inducing
RT ligand (DR4-TRAIL) complex.";
RL Acta Crystallogr. F 71:1273-1281(2015).
CC -!- FUNCTION: Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2,
CC TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG
CC (PubMed:26457518, PubMed:10549288). Induces apoptosis. Its activity may
CC be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3,
CC TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis.
CC {ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:26457518}.
CC -!- SUBUNIT: Homotrimer (PubMed:26457518). One TNFSF10 homotrimer interacts
CC with three TNFSF10A mononers (PubMed:26457518). One TNFSF10 homotrimer
CC interacts with three TNFSF10B mononers (PubMed:10549288).
CC {ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:26457518}.
CC -!- INTERACTION:
CC P50591; Q13618: CUL3; NbExp=2; IntAct=EBI-495373, EBI-456129;
CC P50591; O00220: TNFRSF10A; NbExp=4; IntAct=EBI-495373, EBI-518861;
CC P50591; O14763: TNFRSF10B; NbExp=21; IntAct=EBI-495373, EBI-518882;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14609566};
CC Single-pass type II membrane protein {ECO:0000305}. Secreted
CC {ECO:0000269|PubMed:14609566}. Note=Exists both as membrane-bound and
CC soluble form. {ECO:0000269|PubMed:14609566}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50591-1; Sequence=Displayed;
CC Name=2; Synonyms=TRAIL-short, TRAIL-s;
CC IsoId=P50591-2; Sequence=VSP_043507, VSP_043508;
CC -!- TISSUE SPECIFICITY: Widespread; most predominant in spleen, lung and
CC prostate.
CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC {ECO:0000269|PubMed:25171405}.
CC -!- MISCELLANEOUS: [Isoform 2]: Induced upon HIV infection, antagonizes
CC signaling via TRAIL receptor R2 (TNFRSF10B). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TNFSF10ID42632ch3q26.html";
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DR EMBL; U37518; AAC50332.1; -; mRNA.
DR EMBL; U57059; AAB01233.1; -; mRNA.
DR EMBL; DQ848564; ABI24016.1; -; mRNA.
DR EMBL; EU183231; ABW24658.1; -; mRNA.
DR EMBL; AK296085; BAG58840.1; -; mRNA.
DR EMBL; AC007919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032722; AAH32722.1; -; mRNA.
DR CCDS; CCDS3219.1; -. [P50591-1]
DR CCDS; CCDS54680.1; -. [P50591-2]
DR RefSeq; NP_001177871.1; NM_001190942.1. [P50591-2]
DR RefSeq; NP_003801.1; NM_003810.3. [P50591-1]
DR PDB; 1D0G; X-ray; 2.40 A; A/B/D=114-281.
DR PDB; 1D2Q; X-ray; 2.80 A; A/B=114-281.
DR PDB; 1D4V; X-ray; 2.20 A; B=119-281.
DR PDB; 1DG6; X-ray; 1.30 A; A=91-281.
DR PDB; 1DU3; X-ray; 2.20 A; D/E/F/J/K/L=114-281.
DR PDB; 4N90; X-ray; 3.30 A; A/B/C=114-281.
DR PDB; 5CIR; X-ray; 3.00 A; A/B/D=114-281.
DR PDBsum; 1D0G; -.
DR PDBsum; 1D2Q; -.
DR PDBsum; 1D4V; -.
DR PDBsum; 1DG6; -.
DR PDBsum; 1DU3; -.
DR PDBsum; 4N90; -.
DR PDBsum; 5CIR; -.
DR AlphaFoldDB; P50591; -.
DR SMR; P50591; -.
DR BioGRID; 114280; 92.
DR CORUM; P50591; -.
DR DIP; DIP-6230N; -.
DR IntAct; P50591; 18.
DR MINT; P50591; -.
DR STRING; 9606.ENSP00000241261; -.
DR BindingDB; P50591; -.
DR ChEMBL; CHEMBL5813; -.
DR iPTMnet; P50591; -.
DR PhosphoSitePlus; P50591; -.
DR BioMuta; TNFSF10; -.
DR DMDM; 1730015; -.
DR EPD; P50591; -.
DR jPOST; P50591; -.
DR MassIVE; P50591; -.
DR PaxDb; P50591; -.
DR PeptideAtlas; P50591; -.
DR PRIDE; P50591; -.
DR ProteomicsDB; 56254; -. [P50591-1]
DR Antibodypedia; 3728; 1327 antibodies from 51 providers.
DR DNASU; 8743; -.
DR Ensembl; ENST00000241261.7; ENSP00000241261.2; ENSG00000121858.11. [P50591-1]
DR Ensembl; ENST00000420541.6; ENSP00000389931.2; ENSG00000121858.11. [P50591-2]
DR GeneID; 8743; -.
DR KEGG; hsa:8743; -.
DR MANE-Select; ENST00000241261.7; ENSP00000241261.2; NM_003810.4; NP_003801.1.
DR UCSC; uc003fie.4; human. [P50591-1]
DR CTD; 8743; -.
DR DisGeNET; 8743; -.
DR GeneCards; TNFSF10; -.
DR HGNC; HGNC:11925; TNFSF10.
DR HPA; ENSG00000121858; Low tissue specificity.
DR MIM; 603598; gene.
DR neXtProt; NX_P50591; -.
DR OpenTargets; ENSG00000121858; -.
DR PharmGKB; PA36618; -.
DR VEuPathDB; HostDB:ENSG00000121858; -.
DR eggNOG; ENOG502QQ3R; Eukaryota.
DR GeneTree; ENSGT01050000244878; -.
DR HOGENOM; CLU_070352_1_0_1; -.
DR InParanoid; P50591; -.
DR OMA; CVAVTYM; -.
DR PhylomeDB; P50591; -.
DR TreeFam; TF332169; -.
DR PathwayCommons; P50591; -.
DR Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand.
DR Reactome; R-HSA-3371378; Regulation by c-FLIP.
DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-HSA-5218900; CASP8 activity is inhibited.
DR Reactome; R-HSA-69416; Dimerization of procaspase-8.
DR Reactome; R-HSA-75158; TRAIL signaling.
DR SignaLink; P50591; -.
DR SIGNOR; P50591; -.
DR BioGRID-ORCS; 8743; 20 hits in 1076 CRISPR screens.
DR ChiTaRS; TNFSF10; human.
DR EvolutionaryTrace; P50591; -.
DR GeneWiki; TRAIL; -.
DR GenomeRNAi; 8743; -.
DR Pharos; P50591; Tchem.
DR PRO; PR:P50591; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P50591; protein.
DR Bgee; ENSG00000121858; Expressed in nasal cavity epithelium and 197 other tissues.
DR ExpressionAtlas; P50591; baseline and differential.
DR Genevisible; P50591; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0045569; F:TRAIL binding; IEA:Ensembl.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR021184; TNF_CS.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR017355; TNF_ligand_10/11.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00229; TNF; 1.
DR PIRSF; PIRSF038013; TNF10_TNF11; 1.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS00251; TNF_1; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell membrane; Cytokine;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..281
FT /note="Tumor necrosis factor ligand superfamily member 10"
FT /id="PRO_0000185503"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 124..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between all trimeric partners"
FT /evidence="ECO:0000269|PubMed:10549288,
FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR"
FT VAR_SEQ 91..101
FT /note="MILRTSEETIS -> TPRMKRLWAAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:21859711, ECO:0000303|Ref.4"
FT /id="VSP_043507"
FT VAR_SEQ 102..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:21859711, ECO:0000303|Ref.4"
FT /id="VSP_043508"
FT VARIANT 33
FT /note="V -> I (in dbSNP:rs6763816)"
FT /id="VAR_052584"
FT VARIANT 47
FT /note="D -> E (in dbSNP:rs16845759)"
FT /id="VAR_052585"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1DG6"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1D4V"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1D2Q"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1DG6"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:1D0G"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:1DG6"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1DG6"
FT STRAND 180..193
FT /evidence="ECO:0007829|PDB:1DG6"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5CIR"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:1DG6"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1DG6"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:1DG6"
FT STRAND 237..250
FT /evidence="ECO:0007829|PDB:1DG6"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:1DG6"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1DG6"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:1DG6"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1DG6"
SQ SEQUENCE 281 AA; 32509 MW; DDAAAF78DAAB2F6D CRC64;
MAMMEVQGGP SLGQTCVLIV IFTVLLQSLC VAVTYVYFTN ELKQMQDKYS KSGIACFLKE
DDSYWDPNDE ESMNSPCWQV KWQLRQLVRK MILRTSEETI STVQEKQQNI SPLVRERGPQ
RVAAHITGTR GRSNTLSSPN SKNEKALGRK INSWESSRSG HSFLSNLHLR NGELVIHEKG
FYYIYSQTYF RFQEEIKENT KNDKQMVQYI YKYTSYPDPI LLMKSARNSC WSKDAEYGLY
SIYQGGIFEL KENDRIFVSV TNEHLIDMDH EASFFGAFLV G
