TNF15_HUMAN
ID TNF15_HUMAN Reviewed; 251 AA.
AC O95150; Q3SX69; Q5VJK8; Q5VWH1; Q8NFE9;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 15;
DE AltName: Full=TNF ligand-related molecule 1;
DE AltName: Full=Vascular endothelial cell growth inhibitor;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 15, membrane form;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 15, secreted form;
GN Name=TNFSF15; Synonyms=TL1, VEGI;
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 3), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Umbilical vein;
RX PubMed=9872942; DOI=10.1096/fasebj.13.1.181;
RA Zhai Y., Ni J., Jiang G.-W., Lu J., Xing L., Lincoln C., Carter K.C.,
RA Janat F., Kozak D., Xu S., Rojas L., Aggarwal B.B., Ruben S., Li L.-Y.,
RA Gentz R., Yu G.-L.;
RT "VEGI, a novel cytokine of the tumor necrosis factor family, is an
RT angiogenesis inhibitor that suppresses the growth of colon carcinomas in
RT vivo.";
RL FASEB J. 13:181-189(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11923219; DOI=10.1096/fj.01-0757fje;
RA Chew L.-J., Pan H., Yu J., Tian S., Huang W.-Q., Zhang J.Y., Pang S.,
RA Li L.-Y.;
RT "A novel secreted splice variant of vascular endothelial cell growth
RT inhibitor.";
RL FASEB J. 16:742-744(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF N-TERMINUS,
RP FUNCTION, INTERACTION WITH TNFRSF25 AND TNFRSF6B, SUBCELLULAR LOCATION,
RP PROTEOLYTIC PROCESSING, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11911831; DOI=10.1016/s1074-7613(02)00283-2;
RA Migone T.-S., Zhang J., Luo X., Zhuang L., Chen C., Hu B., Hong J.S.,
RA Perry J.W., Chen S.-F., Zhou J.X.H., Cho Y.H., Ullrich S., Kanakaraj P.,
RA Carrell J., Boyd E., Olsen H.S., Hu G., Pukac L., Liu D., Ni J., Kim S.,
RA Gentz R., Feng P., Moore P.A., Ruben S.M., Wei P.;
RT "TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell
RT costimulator.";
RL Immunity 16:479-492(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 IDENTIFICATION (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=9434163; DOI=10.1016/s0378-1119(97)00509-x;
RA Tan K.B., Harrop J., Reddy M., Young P., Terrett J., Emery J., Moore G.,
RA Truneh A.;
RT "Characterization of a novel TNF-like ligand and recently described TNF
RT ligand and TNF receptor superfamily genes and their constitutive and
RT inducible expression in hematopoietic and non-hematopoietic cells.";
RL Gene 204:35-46(1997).
RN [9]
RP FUNCTION.
RX PubMed=10597252; DOI=10.1038/sj.onc.1203059;
RA Haridas V., Shrivastava A., Su J., Yu G.-L., Ni J., Liu D., Chen S.-F.,
RA Ni Y., Ruben S.M., Gentz R., Aggarwal B.B.;
RT "VEGI, a new member of the TNF family activates nuclear factor-kappa B and
RT c-Jun N-terminal kinase and modulates cell growth.";
RL Oncogene 18:6496-6504(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 71-251, DISULFIDE BOND, AND
RP SUBUNIT.
RX PubMed=17935696; DOI=10.1016/j.bbrc.2007.09.097;
RA Jin T., Guo F., Kim S., Howard A., Zhang Y.-Z.;
RT "X-ray crystal structure of TNF ligand family member TL1A at 2.1A.";
RL Biochem. Biophys. Res. Commun. 364:1-6(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 72-251 IN COMPLEX WITH TNFRSF6B.
RX PubMed=21300286; DOI=10.1016/j.str.2010.12.004;
RA Zhan C., Patskovsky Y., Yan Q., Li Z., Ramagopal U., Cheng H.,
RA Brenowitz M., Hui X., Nathenson S.G., Almo S.C.;
RT "Decoy strategies: the structure of TL1A:DcR3 complex.";
RL Structure 19:162-171(2011).
CC -!- FUNCTION: Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of
CC NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in
CC vitro). Promotes activation of caspases and apoptosis.
CC {ECO:0000269|PubMed:10597252, ECO:0000269|PubMed:11911831,
CC ECO:0000269|PubMed:11923219, ECO:0000269|PubMed:9872942}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17935696,
CC ECO:0000269|PubMed:21300286}.
CC -!- INTERACTION:
CC O95150; O43464: HTRA2; NbExp=3; IntAct=EBI-16355546, EBI-517086;
CC O95150; P42858: HTT; NbExp=3; IntAct=EBI-16355546, EBI-466029;
CC O95150-1; O95407: TNFRSF6B; NbExp=3; IntAct=EBI-15910629, EBI-524171;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:11911831,
CC ECO:0000305|PubMed:11923219}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:11911831, ECO:0000305|PubMed:11923219}.
CC -!- SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member
CC 15, secreted form]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TL1A, VEGI-251;
CC IsoId=O95150-1; Sequence=Displayed;
CC Name=2; Synonyms=VEGI-192;
CC IsoId=O95150-2; Sequence=VSP_033492;
CC Name=3; Synonyms=VEGI-174;
CC IsoId=O95150-3; Sequence=VSP_033493, VSP_033494;
CC -!- TISSUE SPECIFICITY: Specifically expressed in endothelial cells.
CC Detected in monocytes, placenta, lung, liver, kidney, skeletal muscle,
CC pancreas, spleen, prostate, small intestine and colon.
CC {ECO:0000269|PubMed:11911831, ECO:0000269|PubMed:11923219,
CC ECO:0000269|PubMed:9434163, ECO:0000269|PubMed:9872942}.
CC -!- INDUCTION: Up-regulated by IL1A/interleukin-1 alpha and TNF.
CC {ECO:0000269|PubMed:11911831, ECO:0000269|PubMed:11923219}.
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/TNFSF15ID42638ch9q32.html";
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DR EMBL; AF039390; AAD08783.1; -; mRNA.
DR EMBL; AY434464; AAR98573.1; -; mRNA.
DR EMBL; AF520785; AAM77366.1; -; mRNA.
DR EMBL; AK291642; BAF84331.1; -; mRNA.
DR EMBL; AL390240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87431.1; -; Genomic_DNA.
DR EMBL; BC069435; AAH69435.1; -; mRNA.
DR EMBL; BC074940; AAH74940.1; -; mRNA.
DR EMBL; BC074941; AAH74941.1; -; mRNA.
DR EMBL; BC104462; AAI04463.1; -; mRNA.
DR EMBL; BC104463; AAI04464.1; -; mRNA.
DR CCDS; CCDS6809.1; -. [O95150-1]
DR RefSeq; NP_001191273.1; NM_001204344.1. [O95150-2]
DR RefSeq; NP_005109.2; NM_005118.3. [O95150-1]
DR PDB; 2O0O; X-ray; 3.00 A; A/B/C=72-251.
DR PDB; 2QE3; X-ray; 2.50 A; A=72-251.
DR PDB; 2RE9; X-ray; 2.10 A; A/B/C=72-251.
DR PDB; 2RJK; X-ray; 2.30 A; A=72-251.
DR PDB; 2RJL; X-ray; 2.05 A; A=72-251.
DR PDB; 3K51; X-ray; 2.45 A; A=72-251.
DR PDB; 3MI8; X-ray; 2.95 A; A=72-251.
DR PDBsum; 2O0O; -.
DR PDBsum; 2QE3; -.
DR PDBsum; 2RE9; -.
DR PDBsum; 2RJK; -.
DR PDBsum; 2RJL; -.
DR PDBsum; 3K51; -.
DR PDBsum; 3MI8; -.
DR AlphaFoldDB; O95150; -.
DR SMR; O95150; -.
DR BioGRID; 115291; 4.
DR DIP; DIP-59562N; -.
DR IntAct; O95150; 6.
DR STRING; 9606.ENSP00000363157; -.
DR GlyGen; O95150; 2 sites.
DR BioMuta; TNFSF15; -.
DR MassIVE; O95150; -.
DR PaxDb; O95150; -.
DR PeptideAtlas; O95150; -.
DR PRIDE; O95150; -.
DR ProteomicsDB; 50663; -. [O95150-1]
DR ProteomicsDB; 50664; -. [O95150-2]
DR ProteomicsDB; 50665; -. [O95150-3]
DR Antibodypedia; 2153; 712 antibodies from 38 providers.
DR DNASU; 9966; -.
DR Ensembl; ENST00000374045.5; ENSP00000363157.3; ENSG00000181634.8. [O95150-1]
DR GeneID; 9966; -.
DR KEGG; hsa:9966; -.
DR MANE-Select; ENST00000374045.5; ENSP00000363157.3; NM_005118.4; NP_005109.2.
DR UCSC; uc004bjh.4; human. [O95150-1]
DR CTD; 9966; -.
DR DisGeNET; 9966; -.
DR GeneCards; TNFSF15; -.
DR HGNC; HGNC:11931; TNFSF15.
DR HPA; ENSG00000181634; Tissue enhanced (intestine).
DR MalaCards; TNFSF15; -.
DR MIM; 604052; gene.
DR neXtProt; NX_O95150; -.
DR OpenTargets; ENSG00000181634; -.
DR Orphanet; 186; Primary biliary cholangitis.
DR PharmGKB; PA36623; -.
DR VEuPathDB; HostDB:ENSG00000181634; -.
DR eggNOG; ENOG502S4Q1; Eukaryota.
DR GeneTree; ENSGT01050000244957; -.
DR HOGENOM; CLU_070352_3_0_1; -.
DR InParanoid; O95150; -.
DR OMA; QGEACVF; -.
DR PhylomeDB; O95150; -.
DR TreeFam; TF332169; -.
DR PathwayCommons; O95150; -.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; O95150; -.
DR SIGNOR; O95150; -.
DR BioGRID-ORCS; 9966; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; TNFSF15; human.
DR EvolutionaryTrace; O95150; -.
DR GeneWiki; Vascular_endothelial_growth_inhibitor; -.
DR GenomeRNAi; 9966; -.
DR Pharos; O95150; Tbio.
DR PRO; PR:O95150; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O95150; protein.
DR Bgee; ENSG00000181634; Expressed in cartilage tissue and 99 other tissues.
DR ExpressionAtlas; O95150; baseline and differential.
DR Genevisible; O95150; HS.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR006053; TNF.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR008064; TNFSF15.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR11471:SF24; PTHR11471:SF24; 1.
DR Pfam; PF00229; TNF; 1.
DR PRINTS; PR01234; TNECROSISFCT.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..251
FT /note="Tumor necrosis factor ligand superfamily member 15,
FT membrane form"
FT /id="PRO_0000185505"
FT CHAIN 72..251
FT /note="Tumor necrosis factor ligand superfamily member 15,
FT secreted form"
FT /id="PRO_0000333234"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT SITE 71..72
FT /note="Cleavage"
FT SITE 187
FT /note="Important for binding TNFRSF6B"
FT SITE 190
FT /note="Important for binding TNFRSF6B"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 162..202
FT /evidence="ECO:0000269|PubMed:17935696"
FT VAR_SEQ 1..85
FT /note="MAEDLGLSFGETASVEMLPEHGSCRPKARSSSARWALTCCLVLLPFLAGLTT
FT YLLVSQLRAQGEACVQFQALKGQEFAPSHQQVY -> MQLTKGRLHFSHPLSHTKHISP
FT FVTD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11923219"
FT /id="VSP_033492"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9872942"
FT /id="VSP_033493"
FT VAR_SEQ 78..100
FT /note="APSHQQVYAPLRADGDKPRAHLT -> MRRFLSKVYSFPMRKLILFLVFP
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9872942"
FT /id="VSP_033494"
FT VARIANT 110
FT /note="F -> L (in dbSNP:rs16931745)"
FT /id="VAR_043130"
FT CONFLICT 34
FT /note="R -> H (in Ref. 7; AAI04463)"
FT /evidence="ECO:0000305"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2RE9"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2O0O"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2RE9"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:2RE9"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2RE9"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2RJK"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:2RJL"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2RJL"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:2RJL"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:2RJL"
SQ SEQUENCE 251 AA; 28087 MW; 65ED70E367E3446D CRC64;
MAEDLGLSFG ETASVEMLPE HGSCRPKARS SSARWALTCC LVLLPFLAGL TTYLLVSQLR
AQGEACVQFQ ALKGQEFAPS HQQVYAPLRA DGDKPRAHLT VVRQTPTQHF KNQFPALHWE
HELGLAFTKN RMNYTNKFLL IPESGDYFIY SQVTFRGMTS ECSEIRQAGR PNKPDSITVV
ITKVTDSYPE PTQLLMGTKS VCEVGSNWFQ PIYLGAMFSL QEGDKLMVNV SDISLVDYTK
EDKTFFGAFL L
