TNF18_HUMAN
ID TNF18_HUMAN Reviewed; 177 AA.
AC Q9UNG2; A9IQG8; O95852; Q6ISV1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 18 {ECO:0000305};
DE AltName: Full=Activation-inducible TNF-related ligand;
DE Short=AITRL;
DE AltName: Full=Glucocorticoid-induced TNF-related ligand;
DE Short=hGITRL;
GN Name=TNFSF18 {ECO:0000312|HGNC:HGNC:11932}; Synonyms=AITRL, GITRL, TL6;
GN ORFNames=UNQ149/PRO175;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Umbilical vein;
RX PubMed=10074428; DOI=10.1016/s0960-9822(99)80093-1;
RA Gurney A.L., Marsters S.A., Huang R.M., Pitti R.M., Mark D.T.,
RA Baldwin D.T., Gray A.M., Dowd A.D., Brush A.D., Heldens A.D., Schow A.D.,
RA Goddard A.D., Wood W.I., Baker K.P., Godowski P.J., Ashkenazi A.;
RT "Identification of a new member of the tumor necrosis factor family and its
RT receptor, a human ortholog of mouse GITR.";
RL Curr. Biol. 9:215-218(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-177.
RC TISSUE=Brain;
RX PubMed=10037686; DOI=10.1074/jbc.274.10.6056;
RA Kwon B., Yu K.-Y., Ni J., Yu G.-L., Jang I.-K., Kim Y.-J., Xing L., Liu D.,
RA Wang S.-X., Kwon B.S.;
RT "Identification of a novel activation-inducible protein of the tumor
RT necrosis factor receptor superfamily and its ligand.";
RL J. Biol. Chem. 274:6056-6061(1999).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17449724; DOI=10.1189/jlb.0906568;
RA Tuyaerts S., Van Meirvenne S., Bonehill A., Heirman C., Corthals J.,
RA Waldmann H., Breckpot K., Thielemans K., Aerts J.L.;
RT "Expression of human GITRL on myeloid dendritic cells enhances their
RT immunostimulatory function but does not abrogate the suppressive effect of
RT CD4+CD25+ regulatory T cells.";
RL J. Leukoc. Biol. 82:93-105(2007).
RN [9]
RP FUNCTION.
RX PubMed=23892569; DOI=10.1124/jpet.113.207605;
RA Lacal P.M., Petrillo M.G., Ruffini F., Muzi A., Bianchini R., Ronchetti S.,
RA Migliorati G., Riccardi C., Graziani G., Nocentini G.;
RT "Glucocorticoid-induced tumor necrosis factor receptor family-related
RT ligand triggering upregulates vascular cell adhesion molecule-1 and
RT intercellular adhesion molecule-1 and promotes leukocyte adhesion.";
RL J. Pharmacol. Exp. Ther. 347:164-172(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 52-177, FUNCTION, SUBUNIT, AND
RP DISULFIDE BOND.
RX PubMed=18040044; DOI=10.1073/pnas.0709264104;
RA Chattopadhyay K., Ramagopal U.A., Mukhopadhaya A., Malashkevich V.N.,
RA Dilorenzo T.P., Brenowitz M., Nathenson S.G., Almo S.C.;
RT "Assembly and structural properties of glucocorticoid-induced TNF receptor
RT ligand: implications for function.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19452-19457(2007).
CC -!- FUNCTION: Cytokine that binds to TNFRSF18/AITR/GITR. Regulates T-cell
CC responses. Can function as costimulator and lower the threshold for T-
CC cell activation and T-cell proliferation. Important for interactions
CC between activated T-lymphocytes and endothelial cells. Mediates
CC activation of NF-kappa-B. Triggers increased phosphorylation of STAT1
CC and up-regulates expression of VCAM1 and ICAM1 (PubMed:23892569).
CC Promotes leukocyte adhesion to endothelial cells (PubMed:23892569).
CC Regulates migration of monocytes from the splenic reservoir to sites of
CC inflammation (By similarity). {ECO:0000250|UniProtKB:Q7TS55,
CC ECO:0000269|PubMed:17449724, ECO:0000269|PubMed:18040044,
CC ECO:0000269|PubMed:23892569}.
CC -!- SUBUNIT: Homodimer (By similarity). Homotrimer. {ECO:0000250,
CC ECO:0000269|PubMed:18040044}.
CC -!- INTERACTION:
CC Q9UNG2; Q2M3D2: EXOC3L2; NbExp=3; IntAct=EBI-15672281, EBI-14890134;
CC Q9UNG2; Q9Y5U5: TNFRSF18; NbExp=2; IntAct=EBI-15672281, EBI-3962532;
CC Q9UNG2; Q9UNG2: TNFSF18; NbExp=7; IntAct=EBI-15672281, EBI-15672281;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17449724};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:17449724}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the small intestine,
CC ovary, testis, kidney and endothelial cells.
CC -!- INDUCTION: Up-regulated after stimulation by bacterial
CC lipopolysaccharides (LPS).
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/TNFSF18ID42639ch1q25.html";
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DR EMBL; AL031599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90937.1; -; Genomic_DNA.
DR EMBL; BC069111; AAH69111.1; -; mRNA.
DR EMBL; BC069319; AAH69319.1; -; mRNA.
DR EMBL; BC093986; AAH93986.1; -; mRNA.
DR EMBL; BC112032; AAI12033.1; -; mRNA.
DR EMBL; AK313273; BAG36082.1; -; mRNA.
DR EMBL; AY358868; AAQ89227.1; -; mRNA.
DR EMBL; AF125303; AAD22634.1; -; mRNA.
DR EMBL; AF117713; AAD19695.1; -; mRNA.
DR CCDS; CCDS1305.2; -.
DR RefSeq; NP_005083.2; NM_005092.3.
DR PDB; 2Q1M; X-ray; 2.30 A; A=52-177.
DR PDB; 2R30; X-ray; 3.20 A; A=52-177.
DR PDB; 2R32; X-ray; 1.95 A; A=52-177.
DR PDB; 3B93; X-ray; 2.20 A; A/B/C=50-177.
DR PDB; 3B94; X-ray; 2.50 A; A/B/C/D=50-177.
DR PDB; 7KHD; X-ray; 2.96 A; A/B=50-177.
DR PDB; 7LAW; X-ray; 2.75 A; A/B=50-177.
DR PDBsum; 2Q1M; -.
DR PDBsum; 2R30; -.
DR PDBsum; 2R32; -.
DR PDBsum; 3B93; -.
DR PDBsum; 3B94; -.
DR PDBsum; 7KHD; -.
DR PDBsum; 7LAW; -.
DR AlphaFoldDB; Q9UNG2; -.
DR BioGRID; 114476; 71.
DR DIP; DIP-29882N; -.
DR IntAct; Q9UNG2; 2.
DR STRING; 9606.ENSP00000385470; -.
DR GlyGen; Q9UNG2; 2 sites.
DR BioMuta; TNFSF18; -.
DR DMDM; 325511353; -.
DR MassIVE; Q9UNG2; -.
DR PaxDb; Q9UNG2; -.
DR PeptideAtlas; Q9UNG2; -.
DR PRIDE; Q9UNG2; -.
DR ProteomicsDB; 85288; -.
DR Antibodypedia; 2126; 598 antibodies from 37 providers.
DR DNASU; 8995; -.
DR Ensembl; ENST00000404377.5; ENSP00000385470.4; ENSG00000120337.10.
DR GeneID; 8995; -.
DR KEGG; hsa:8995; -.
DR MANE-Select; ENST00000404377.5; ENSP00000385470.4; NM_005092.4; NP_005083.3.
DR UCSC; uc001giu.3; human.
DR CTD; 8995; -.
DR DisGeNET; 8995; -.
DR GeneCards; TNFSF18; -.
DR HGNC; HGNC:11932; TNFSF18.
DR HPA; ENSG00000120337; Tissue enhanced (gallbladder).
DR MIM; 603898; gene.
DR neXtProt; NX_Q9UNG2; -.
DR OpenTargets; ENSG00000120337; -.
DR PharmGKB; PA36624; -.
DR VEuPathDB; HostDB:ENSG00000120337; -.
DR eggNOG; ENOG502SWIC; Eukaryota.
DR GeneTree; ENSGT00390000002560; -.
DR HOGENOM; CLU_134507_0_0_1; -.
DR InParanoid; Q9UNG2; -.
DR OMA; YKEPAPF; -.
DR OrthoDB; 1513112at2759; -.
DR PhylomeDB; Q9UNG2; -.
DR TreeFam; TF338614; -.
DR PathwayCommons; Q9UNG2; -.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; Q9UNG2; -.
DR BioGRID-ORCS; 8995; 11 hits in 1072 CRISPR screens.
DR EvolutionaryTrace; Q9UNG2; -.
DR GeneWiki; TNFSF18; -.
DR GenomeRNAi; 8995; -.
DR Pharos; Q9UNG2; Tbio.
DR PRO; PR:Q9UNG2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UNG2; protein.
DR Bgee; ENSG00000120337; Expressed in gall bladder and 78 other tissues.
DR Genevisible; Q9UNG2; HS.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR GO; GO:2000329; P:negative regulation of T-helper 17 cell lineage commitment; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
DR GO; GO:2000508; P:regulation of dendritic cell chemotaxis; IEA:Ensembl.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0042129; P:regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0002309; P:T cell proliferation involved in immune response; ISS:UniProtKB.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR042380; TNFSF18.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15267; PTHR15267; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Cytokine; Disulfide bond;
KW Glycoprotein; Immunity; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..177
FT /note="Tumor necrosis factor ligand superfamily member 18"
FT /id="PRO_0000185506"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..78
FT /evidence="ECO:0000269|PubMed:18040044"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2R32"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:7KHD"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3B93"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2R32"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2R32"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:2R32"
SQ SEQUENCE 177 AA; 20308 MW; 3D78CE6B90F4C9E3 CRC64;
MCLSHLENMP LSHSRTQGAQ RSSWKLWLFC SIVMLLFLCS FSWLIFIFLQ LETAKEPCMA
KFGPLPSKWQ MASSEPPCVN KVSDWKLEIL QNGLYLIYGQ VAPNANYNDV APFEVRLYKN
KDMIQTLTNK SKIQNVGGTY ELHVGDTIDL IFNSEHQVLK NNTYWGIILL ANPQFIS
