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TNR19_HUMAN
ID   TNR19_HUMAN             Reviewed;         423 AA.
AC   Q9NS68; A8KA09; A8KA26; B1AM40; B1AM41; B4E2I6; Q9BXZ9; Q9BY00; Q9NZV2;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 19;
DE   AltName: Full=TRADE;
DE   AltName: Full=Toxicity and JNK inducer;
DE   Flags: Precursor;
GN   Name=TNFRSF19; Synonyms=TAJ, TROY; ORFNames=UNQ1888/PRO4333;
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), AND INTERACTION WITH TRAF1; TRAF2;
RP   TRAF3 AND TRAF5.
RC   TISSUE=Fetal spleen;
RX   PubMed=10809768; DOI=10.1074/jbc.275.20.15336;
RA   Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.;
RT   "TAJ, a novel member of the tumor necrosis factor receptor family,
RT   activates the c-Jun N-terminal kinase pathway and mediates caspase-
RT   independent cell death.";
RL   J. Biol. Chem. 275:15336-15342(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Glial tumor;
RX   PubMed=10764796; DOI=10.1074/jbc.m002691200;
RA   Kojima T., Morikawa Y., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA   Senba E., Kitamura T.;
RT   "TROY, a newly identified member of the tumor necrosis factor receptor
RT   superfamily, exhibits a homology with Edar and is expressed in embryonic
RT   skin and hair follicles.";
RL   J. Biol. Chem. 275:20742-20747(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS THR-31 AND
RP   ILE-405.
RA   Chaudhary D., Long A.J.;
RT   "TRADE, a novel TNF receptor family member associated with death
RT   signaling.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS VAL-159
RP   AND ILE-405.
RC   TISSUE=Trachea;
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=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [9]
RP   PROTEIN SEQUENCE OF 30-44.
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   [10]
RP   INTERACTION WITH LINGO1.
RX   PubMed=15694321; DOI=10.1016/j.neuron.2004.12.040;
RA   Park J.B., Yiu G., Kaneko S., Wang J., Chang J., He X.L., Garcia K.C.,
RA   He Z.;
RT   "A TNF receptor family member, TROY, is a coreceptor with Nogo receptor in
RT   mediating the inhibitory activity of myelin inhibitors.";
RL   Neuron 45:345-351(2005).
CC   -!- FUNCTION: Can mediate activation of JNK and NF-kappa-B. May promote
CC       caspase-independent cell death.
CC   -!- SUBUNIT: Associates with TRAF1, TRAF2, TRAF3 and TRAF5. Interacts with
CC       LINGO1. {ECO:0000269|PubMed:10809768, ECO:0000269|PubMed:15694321}.
CC   -!- INTERACTION:
CC       Q9NS68; P52565: ARHGDIA; NbExp=3; IntAct=EBI-530381, EBI-712693;
CC       Q9NS68; P30086: PEBP1; NbExp=4; IntAct=EBI-530381, EBI-716384;
CC       Q9NS68; P35232: PHB; NbExp=3; IntAct=EBI-530381, EBI-354213;
CC       Q9NS68-2; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-12089038, EBI-6166686;
CC       Q9NS68-2; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-12089038, EBI-11980301;
CC       Q9NS68-2; O43765: SGTA; NbExp=3; IntAct=EBI-12089038, EBI-347996;
CC       Q9NS68-2; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-12089038, EBI-744081;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=TAJ-alpha, TRADEalpha;
CC         IsoId=Q9NS68-1; Sequence=Displayed;
CC       Name=2; Synonyms=TRADEbeta;
CC         IsoId=Q9NS68-2; Sequence=VSP_006512;
CC       Name=3;
CC         IsoId=Q9NS68-3; Sequence=VSP_044886, VSP_006512;
CC   -!- TISSUE SPECIFICITY: Highly expressed in prostate. Detected at lower
CC       levels in thymus, spleen, testis, uterus, small intestine, colon and
CC       peripheral blood leukocytes.
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DR   EMBL; AF167555; AAF71828.1; -; mRNA.
DR   EMBL; AB040434; BAB03269.1; -; mRNA.
DR   EMBL; AF246998; AAK28395.1; -; mRNA.
DR   EMBL; AF246999; AAK28396.1; -; mRNA.
DR   EMBL; AY358888; AAQ89247.1; -; mRNA.
DR   EMBL; AK292874; BAF85563.1; -; mRNA.
DR   EMBL; AK292891; BAF85580.1; -; mRNA.
DR   EMBL; AK304290; BAG65148.1; -; mRNA.
DR   EMBL; AL161422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471075; EAX08326.1; -; Genomic_DNA.
DR   EMBL; BC047321; AAH47321.1; -; mRNA.
DR   CCDS; CCDS55893.1; -. [Q9NS68-3]
DR   CCDS; CCDS9301.1; -. [Q9NS68-2]
DR   CCDS; CCDS9302.1; -. [Q9NS68-1]
DR   RefSeq; NP_001191387.1; NM_001204458.1. [Q9NS68-2]
DR   RefSeq; NP_001191388.1; NM_001204459.1. [Q9NS68-3]
DR   RefSeq; NP_061117.2; NM_018647.3. [Q9NS68-1]
DR   RefSeq; NP_683760.1; NM_148957.3. [Q9NS68-2]
DR   RefSeq; XP_005266502.1; XM_005266445.2. [Q9NS68-1]
DR   RefSeq; XP_011533448.1; XM_011535146.1. [Q9NS68-1]
DR   RefSeq; XP_016876140.1; XM_017020651.1. [Q9NS68-1]
DR   AlphaFoldDB; Q9NS68; -.
DR   BioGRID; 120684; 61.
DR   CORUM; Q9NS68; -.
DR   IntAct; Q9NS68; 48.
DR   MINT; Q9NS68; -.
DR   STRING; 9606.ENSP00000371693; -.
DR   GlyGen; Q9NS68; 1 site.
DR   iPTMnet; Q9NS68; -.
DR   PhosphoSitePlus; Q9NS68; -.
DR   BioMuta; TNFRSF19; -.
DR   DMDM; 21264102; -.
DR   jPOST; Q9NS68; -.
DR   MassIVE; Q9NS68; -.
DR   MaxQB; Q9NS68; -.
DR   PaxDb; Q9NS68; -.
DR   PeptideAtlas; Q9NS68; -.
DR   PRIDE; Q9NS68; -.
DR   ProteomicsDB; 82498; -. [Q9NS68-1]
DR   ProteomicsDB; 82499; -. [Q9NS68-2]
DR   Antibodypedia; 2432; 379 antibodies from 33 providers.
DR   DNASU; 55504; -.
DR   Ensembl; ENST00000248484.9; ENSP00000248484.4; ENSG00000127863.16. [Q9NS68-2]
DR   Ensembl; ENST00000382258.8; ENSP00000371693.4; ENSG00000127863.16. [Q9NS68-1]
DR   Ensembl; ENST00000382263.3; ENSP00000371698.3; ENSG00000127863.16. [Q9NS68-2]
DR   Ensembl; ENST00000403372.6; ENSP00000385408.2; ENSG00000127863.16. [Q9NS68-3]
DR   GeneID; 55504; -.
DR   KEGG; hsa:55504; -.
DR   MANE-Select; ENST00000248484.9; ENSP00000248484.4; NM_148957.4; NP_683760.1. [Q9NS68-2]
DR   UCSC; uc001uot.4; human. [Q9NS68-1]
DR   CTD; 55504; -.
DR   DisGeNET; 55504; -.
DR   GeneCards; TNFRSF19; -.
DR   HGNC; HGNC:11915; TNFRSF19.
DR   HPA; ENSG00000127863; Tissue enhanced (salivary gland, skin).
DR   MIM; 606122; gene.
DR   neXtProt; NX_Q9NS68; -.
DR   OpenTargets; ENSG00000127863; -.
DR   PharmGKB; PA36608; -.
DR   VEuPathDB; HostDB:ENSG00000127863; -.
DR   eggNOG; ENOG502QQHI; Eukaryota.
DR   GeneTree; ENSGT00940000153259; -.
DR   HOGENOM; CLU_050058_0_0_1; -.
DR   InParanoid; Q9NS68; -.
DR   OMA; SHSCAFH; -.
DR   PhylomeDB; Q9NS68; -.
DR   TreeFam; TF331385; -.
DR   PathwayCommons; Q9NS68; -.
DR   SignaLink; Q9NS68; -.
DR   BioGRID-ORCS; 55504; 6 hits in 1065 CRISPR screens.
DR   ChiTaRS; TNFRSF19; human.
DR   GeneWiki; TNFRSF19; -.
DR   GenomeRNAi; 55504; -.
DR   Pharos; Q9NS68; Tbio.
DR   PRO; PR:Q9NS68; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q9NS68; protein.
DR   Bgee; ENSG00000127863; Expressed in upper arm skin and 157 other tissues.
DR   ExpressionAtlas; Q9NS68; baseline and differential.
DR   Genevisible; Q9NS68; HS.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0005031; F:tumor necrosis factor receptor activity; NAS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR   GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0007254; P:JNK cascade; NAS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR   CDD; cd13418; TNFRSF19; 1.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR022342; TNFR_19.
DR   InterPro; IPR034047; TNFRSF19_N.
DR   PANTHER; PTHR12120:SF1; PTHR12120:SF1; 1.
DR   Pfam; PF00020; TNFR_c6; 2.
DR   PRINTS; PR01969; TNFACTORR19.
DR   SMART; SM00208; TNFR; 2.
DR   PROSITE; PS00652; TNFR_NGFR_1; 2.
DR   PROSITE; PS50050; TNFR_NGFR_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           30..423
FT                   /note="Tumor necrosis factor receptor superfamily member
FT                   19"
FT                   /id="PRO_0000034597"
FT   TOPO_DOM        30..170
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..423
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          33..72
FT                   /note="TNFR-Cys 1"
FT   REPEAT          74..114
FT                   /note="TNFR-Cys 2"
FT   REPEAT          116..149
FT                   /note="TNFR-Cys 3"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        49..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        52..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        75..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        92..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        95..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        117..135
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        138..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   VAR_SEQ         1..132
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044886"
FT   VAR_SEQ         416..423
FT                   /note="VRQRLGSL -> EA (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12975309,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|Ref.3"
FT                   /id="VSP_006512"
FT   VARIANT         31
FT                   /note="S -> T (in dbSNP:rs9550987)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_024278"
FT   VARIANT         159
FT                   /note="A -> V (in dbSNP:rs61756242)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_070812"
FT   VARIANT         405
FT                   /note="V -> I (in dbSNP:rs3751362)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT                   /id="VAR_024279"
FT   CONFLICT        74
FT                   /note="T -> A (in Ref. 1; AAF71828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215..216
FT                   /note="GS -> ET (in Ref. 1; AAF71828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="F -> L (in Ref. 3; AAK28396)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="T -> A (in Ref. 3; AAK28396)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   423 AA;  46015 MW;  B5891CEA9ED45361 CRC64;
     MALKVLLEQE KTFFTLLVLL GYLSCKVTCE SGDCRQQEFR DRSGNCVPCN QCGPGMELSK
     ECGFGYGEDA QCVTCRLHRF KEDWGFQKCK PCLDCAVVNR FQKANCSATS DAICGDCLPG
     FYRKTKLVGF QDMECVPCGD PPPPYEPHCA SKVNLVKIAS TASSPRDTAL AAVICSALAT
     VLLALLILCV IYCKRQFMEK KPSWSLRSQD IQYNGSELSC FDRPQLHEYA HRACCQCRRD
     SVQTCGPVRL LPSMCCEEAC SPNPATLGCG VHSAASLQAR NAGPAGEMVP TFFGSLTQSI
     CGEFSDAWPL MQNPMGGDNI SFCDSYPELT GEDIHSLNPE LESSTSLDSN SSQDLVGGAV
     PVQSHSENFT AATDLSRYNN TLVESASTQD ALTMRSQLDQ ESGAVIHPAT QTSLQVRQRL
     GSL
 
 
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