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I17RD_HUMAN
ID   I17RD_HUMAN             Reviewed;         739 AA.
AC   Q8NFM7; Q2NKP7; Q58EZ7; Q6RVF4; Q6UWI5; Q8N113; Q8NFS0; Q9UFA0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 3.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Interleukin-17 receptor D;
DE            Short=IL-17 receptor D;
DE            Short=IL-17RD;
DE   AltName: Full=IL17Rhom;
DE   AltName: Full=Interleukin-17 receptor-like protein;
DE   AltName: Full=Sef homolog;
DE            Short=hSef;
DE   Flags: Precursor;
GN   Name=IL17RD; Synonyms=IL17RLM, SEF; ORFNames=UNQ6115/PRO20026;
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] (ISOFORMS 1 AND 2), VARIANT MET-255, FUNCTION,
RP   AND INTERACTION WITH FGFR1 AND FGFR2.
RX   PubMed=12958313; DOI=10.1074/jbc.m306936200;
RA   Xiong S.Q., Zhao Q.H., Rong Z., Huang G.R., Huang Y., Chen P.L., Zhang S.,
RA   Liu L., Chang Z.J.;
RT   "hSef inhibits PC-12 cell differentiation by interfering with Ras-mitogen-
RT   activated protein kinase MAPK signaling.";
RL   J. Biol. Chem. 278:50273-50282(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT MET-255, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Testis;
RX   PubMed=14742870; DOI=10.1073/pnas.0307952100;
RA   Preger E., Ziv I., Shabtay A., Sher I., Tsang M., Dawid I.B., Altuvia Y.,
RA   Ron D.;
RT   "Alternative splicing generates an isoform of the human Sef gene with
RT   altered subcellular localization and specificity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:1229-1234(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-255.
RA   Gilbert J.M., Gorman D.M.;
RT   "Identification of novel IL-17 related receptors.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-255.
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 2), AND VARIANT MET-255.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT MET-255.
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   FUNCTION, TISSUE SPECIFICITY, HOMOOLIGOMERIZATION, AND INTERACTION WITH
RP   FGFR1.
RX   PubMed=12807873; DOI=10.1074/jbc.m305022200;
RA   Yang R.-B., Domingos Ng C.K., Wasserman S.M., Koemueves L.G.,
RA   Gerritsen M.E., Topper J.N.;
RT   "A novel interleukin-17 receptor-like protein identified in human umbilical
RT   vein endothelial cells antagonizes basic fibroblast growth factor-induced
RT   signaling.";
RL   J. Biol. Chem. 278:33232-33238(2003).
RN   [8]
RP   FUNCTION, INTERACTION WITH MAP2K1/2, AND IDENTIFICATION IN A COMPLEX WITH
RP   MAP2K1/2 AND MAPK1/3.
RX   PubMed=15239952; DOI=10.1016/j.devcel.2004.05.019;
RA   Torii S., Kusakabe M., Yamamoto T., Maekawa M., Nishida E.;
RT   "Sef is a spatial regulator for Ras/MAP kinase signaling.";
RL   Dev. Cell 7:33-44(2004).
RN   [9]
RP   VARIANTS HH18 THR-131; ARG-162; SER-306; CYS-379; LEU-468; GLN-577 AND
RP   VAL-735, AND CHARACTERIZATION OF VARIANTS HH18 THR-131; ARG-162; SER-306;
RP   CYS-379; LEU-468; GLN-577 AND VAL-735.
RX   PubMed=23643382; DOI=10.1016/j.ajhg.2013.04.008;
RA   Miraoui H., Dwyer A.A., Sykiotis G.P., Plummer L., Chung W., Feng B.,
RA   Beenken A., Clarke J., Pers T.H., Dworzynski P., Keefe K., Niedziela M.,
RA   Raivio T., Crowley W.F. Jr., Seminara S.B., Quinton R., Hughes V.A.,
RA   Kumanov P., Young J., Yialamas M.A., Hall J.E., Van Vliet G.,
RA   Chanoine J.P., Rubenstein J., Mohammadi M., Tsai P.S., Sidis Y., Lage K.,
RA   Pitteloud N.;
RT   "Mutations in FGF17, IL17RD, DUSP6, SPRY4, and FLRT3 are identified in
RT   individuals with congenital hypogonadotropic hypogonadism.";
RL   Am. J. Hum. Genet. 92:725-743(2013).
CC   -!- FUNCTION: Feedback inhibitor of fibroblast growth factor mediated Ras-
CC       MAPK signaling and ERK activation (PubMed:12958313, PubMed:12807873).
CC       Regulates the nuclear ERK signaling pathway by spatially blocking
CC       nuclear translocation of activated ERK without inhibiting cytoplasmic
CC       phosphorylation of ERK (PubMed:15239952). Mediates JNK activation and
CC       may be involved in apoptosis (By similarity). May inhibit FGF-induced
CC       FGFR1 tyrosine phosphorylation (By similarity). Might have a role in
CC       the early stages of fate specification of GnRH-secreting neurons (By
CC       similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition
CC       in lens epithelial cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q8JZL1, ECO:0000269|PubMed:12807873,
CC       ECO:0000269|PubMed:12958313, ECO:0000269|PubMed:15239952}.
CC   -!- SUBUNIT: Interacts with MAP3K7 (By similarity). Self-associates.
CC       Interacts with FGFR1, FGFR2 and phosphorylated MAP2K1 or MAP2K2.
CC       Associates with a MAP2K1/2-MAPK1/3 complex. {ECO:0000250,
CC       ECO:0000269|PubMed:12807873, ECO:0000269|PubMed:12958313,
CC       ECO:0000269|PubMed:15239952}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:14742870}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:14742870}. Cell membrane
CC       {ECO:0000269|PubMed:14742870}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:14742870}. Note=Predominantly associated with the
CC       Golgi apparatus and is partially translocated to the plasma membrane
CC       upon stimulation.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=hSef-a, IL17RLM-L, Long;
CC         IsoId=Q8NFM7-1; Sequence=Displayed;
CC       Name=2; Synonyms=IL17RLM-S, Short;
CC         IsoId=Q8NFM7-2; Sequence=VSP_015582;
CC       Name=3;
CC         IsoId=Q8NFM7-3; Sequence=VSP_015583;
CC       Name=4; Synonyms=hSef-b;
CC         IsoId=Q8NFM7-4; Sequence=VSP_015584;
CC   -!- TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells and
CC       in several highly vascularized tissues such as kidney, colon, skeletal
CC       muscle, heart and small intestine. Highly expressed in ductal
CC       epithelial cells of salivary glands, seminal vesicles and the
CC       collecting tubules of the kidney. Isoform 1 is also highly expressed in
CC       both fetal and adult brain, pituitary, tonsils, spleen, adenoids, fetal
CC       kidney, liver, testes and ovary. Isoform 1 is also expressed at
CC       moderate levels in primary aortic endothelial cells and adrenal
CC       medulla, and at low levels in adrenal cortex. Isoform 4 is specifically
CC       and highly expressed in pituitary, fetal brain and umbilical vein
CC       endothelial cells. {ECO:0000269|PubMed:12807873}.
CC   -!- DISEASE: Hypogonadotropic hypogonadism 18 with or without anosmia
CC       (HH18) [MIM:615267]: A disorder characterized by absent or incomplete
CC       sexual maturation by the age of 18 years, in conjunction with low
CC       levels of circulating gonadotropins and testosterone and no other
CC       abnormalities of the hypothalamic-pituitary axis. In some cases, it is
CC       associated with non-reproductive phenotypes, such as anosmia, cleft
CC       palate, and sensorineural hearing loss. Anosmia or hyposmia is related
CC       to the absence or hypoplasia of the olfactory bulbs and tracts.
CC       Hypogonadism is due to deficiency in gonadotropin-releasing hormone and
CC       probably results from a failure of embryonic migration of gonadotropin-
CC       releasing hormone-synthesizing neurons. In the presence of anosmia,
CC       idiopathic hypogonadotropic hypogonadism is referred to as Kallmann
CC       syndrome, whereas in the presence of a normal sense of smell, it has
CC       been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH).
CC       {ECO:0000269|PubMed:23643382}. Note=The disease is caused by variants
CC       affecting distinct genetic loci, including the gene represented in this
CC       entry. Some patients carrying mutations in IL17RD also have a
CC       heterozygous mutation in another HH-associated gene including FGFR1 and
CC       KISS1R (PubMed:23643382). {ECO:0000269|PubMed:23643382}.
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DR   EMBL; AF494208; AAM74077.1; -; mRNA.
DR   EMBL; AF494211; AAM74080.1; -; mRNA.
DR   EMBL; AY489047; AAS15051.2; -; mRNA.
DR   EMBL; AF458067; AAM77571.1; -; mRNA.
DR   EMBL; AY358774; AAQ89134.1; -; mRNA.
DR   EMBL; AL133097; CAB61408.1; -; mRNA.
DR   EMBL; AL833913; CAD38769.1; -; mRNA.
DR   EMBL; BC111702; AAI11703.2; -; mRNA.
DR   CCDS; CCDS2880.2; -. [Q8NFM7-1]
DR   CCDS; CCDS82790.1; -. [Q8NFM7-2]
DR   PIR; T42695; T42695.
DR   RefSeq; NP_001305793.1; NM_001318864.1. [Q8NFM7-2]
DR   RefSeq; NP_060033.3; NM_017563.4. [Q8NFM7-1]
DR   RefSeq; XP_006713272.1; XM_006713209.3.
DR   RefSeq; XP_011532151.2; XM_011533849.2. [Q8NFM7-2]
DR   AlphaFoldDB; Q8NFM7; -.
DR   SMR; Q8NFM7; -.
DR   BioGRID; 120132; 26.
DR   IntAct; Q8NFM7; 6.
DR   MINT; Q8NFM7; -.
DR   STRING; 9606.ENSP00000296318; -.
DR   GlyGen; Q8NFM7; 8 sites.
DR   iPTMnet; Q8NFM7; -.
DR   PhosphoSitePlus; Q8NFM7; -.
DR   BioMuta; IL17RD; -.
DR   DMDM; 126302555; -.
DR   EPD; Q8NFM7; -.
DR   MassIVE; Q8NFM7; -.
DR   PaxDb; Q8NFM7; -.
DR   PeptideAtlas; Q8NFM7; -.
DR   PRIDE; Q8NFM7; -.
DR   ProteomicsDB; 73324; -. [Q8NFM7-1]
DR   ProteomicsDB; 73325; -. [Q8NFM7-2]
DR   ProteomicsDB; 73326; -. [Q8NFM7-3]
DR   ProteomicsDB; 73327; -. [Q8NFM7-4]
DR   Antibodypedia; 31518; 317 antibodies from 31 providers.
DR   DNASU; 54756; -.
DR   Ensembl; ENST00000296318.12; ENSP00000296318.7; ENSG00000144730.19. [Q8NFM7-1]
DR   Ensembl; ENST00000320057.9; ENSP00000322250.5; ENSG00000144730.19. [Q8NFM7-2]
DR   Ensembl; ENST00000463523.5; ENSP00000417516.1; ENSG00000144730.19. [Q8NFM7-2]
DR   GeneID; 54756; -.
DR   KEGG; hsa:54756; -.
DR   MANE-Select; ENST00000296318.12; ENSP00000296318.7; NM_017563.5; NP_060033.3.
DR   UCSC; uc003dil.3; human. [Q8NFM7-1]
DR   CTD; 54756; -.
DR   DisGeNET; 54756; -.
DR   GeneCards; IL17RD; -.
DR   GeneReviews; IL17RD; -.
DR   HGNC; HGNC:17616; IL17RD.
DR   HPA; ENSG00000144730; Tissue enhanced (choroid).
DR   MalaCards; IL17RD; -.
DR   MIM; 606807; gene.
DR   MIM; 615267; phenotype.
DR   neXtProt; NX_Q8NFM7; -.
DR   OpenTargets; ENSG00000144730; -.
DR   Orphanet; 478; Kallmann syndrome.
DR   PharmGKB; PA134993407; -.
DR   VEuPathDB; HostDB:ENSG00000144730; -.
DR   eggNOG; ENOG502QV61; Eukaryota.
DR   GeneTree; ENSGT00940000156669; -.
DR   HOGENOM; CLU_024846_0_0_1; -.
DR   InParanoid; Q8NFM7; -.
DR   OMA; DFCLKAE; -.
DR   PhylomeDB; Q8NFM7; -.
DR   TreeFam; TF329644; -.
DR   PathwayCommons; Q8NFM7; -.
DR   Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR   SignaLink; Q8NFM7; -.
DR   BioGRID-ORCS; 54756; 14 hits in 1068 CRISPR screens.
DR   ChiTaRS; IL17RD; human.
DR   GenomeRNAi; 54756; -.
DR   Pharos; Q8NFM7; Tbio.
DR   PRO; PR:Q8NFM7; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8NFM7; protein.
DR   Bgee; ENSG00000144730; Expressed in secondary oocyte and 171 other tissues.
DR   ExpressionAtlas; Q8NFM7; baseline and differential.
DR   Genevisible; Q8NFM7; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030368; F:interleukin-17 receptor activity; IBA:GO_Central.
DR   GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR039465; IL-17_rcpt-like.
DR   InterPro; IPR031951; IL17R_D_N.
DR   InterPro; IPR013568; SEFIR_dom.
DR   InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR   PANTHER; PTHR15583; PTHR15583; 1.
DR   Pfam; PF16742; IL17R_D_N; 1.
DR   Pfam; PF08357; SEFIR; 1.
DR   SUPFAM; SSF52200; SSF52200; 1.
DR   PROSITE; PS51534; SEFIR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Disease variant;
KW   Glycoprotein; Golgi apparatus; Hypogonadotropic hypogonadism;
KW   Kallmann syndrome; Membrane; Receptor; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..739
FT                   /note="Interleukin-17 receptor D"
FT                   /id="PRO_0000041871"
FT   TOPO_DOM        17..299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..739
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          355..509
FT                   /note="SEFIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
FT   REGION          614..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..144
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12958313,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_015582"
FT   VAR_SEQ         1..42
FT                   /note="MAPWLQLCSVFFTVNACLNGSQLAVAAGGSGRARGADTCGWR -> MPRASA
FT                   SGVPALFVSGEQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_015583"
FT   VAR_SEQ         1..42
FT                   /note="MAPWLQLCSVFFTVNACLNGSQLAVAAGGSGRARGADTCGWR -> MDYRQS
FT                   WPWQ (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14742870,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015584"
FT   VARIANT         131
FT                   /note="K -> T (in HH18; results in decreased expression at
FT                   the cell surface and reduced activity; dbSNP:rs184758350)"
FT                   /evidence="ECO:0000269|PubMed:23643382"
FT                   /id="VAR_069936"
FT   VARIANT         162
FT                   /note="K -> R (in HH18; results in decreased expression at
FT                   the cell surface)"
FT                   /evidence="ECO:0000269|PubMed:23643382"
FT                   /id="VAR_069937"
FT   VARIANT         255
FT                   /note="T -> M (in dbSNP:rs6780995)"
FT                   /evidence="ECO:0000269|PubMed:12958313,
FT                   ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14742870,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_023478"
FT   VARIANT         301
FT                   /note="V -> M (in dbSNP:rs17057718)"
FT                   /id="VAR_023479"
FT   VARIANT         306
FT                   /note="P -> S (in HH18; reduced activity)"
FT                   /evidence="ECO:0000269|PubMed:23643382"
FT                   /id="VAR_069938"
FT   VARIANT         379
FT                   /note="Y -> C (in HH18; rare variant associated with
FT                   susceptibility to disease; some patients have a second
FT                   mutation in the HH-associated gene FGFR1; reduced activity;
FT                   dbSNP:rs369641068)"
FT                   /evidence="ECO:0000269|PubMed:23643382"
FT                   /id="VAR_069939"
FT   VARIANT         468
FT                   /note="S -> L (in HH18; reduced activity;
FT                   dbSNP:rs145221454)"
FT                   /evidence="ECO:0000269|PubMed:23643382"
FT                   /id="VAR_069940"
FT   VARIANT         577
FT                   /note="P -> Q (in HH18; reduced activity;
FT                   dbSNP:rs587776980)"
FT                   /evidence="ECO:0000269|PubMed:23643382"
FT                   /id="VAR_069941"
FT   VARIANT         735
FT                   /note="A -> V (in HH18; rare variant associated with
FT                   susceptibility to disease; the patient carries a second
FT                   mutation in the HH-associated gene KISS1R; results in
FT                   decreased expression at the cell surface;
FT                   dbSNP:rs587776979)"
FT                   /evidence="ECO:0000269|PubMed:23643382"
FT                   /id="VAR_069942"
FT   CONFLICT        223
FT                   /note="H -> HGSDMQVSFDHAPH (in Ref. 4; CAB61408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="K -> E (in Ref. 1; AAM74077)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   739 AA;  82411 MW;  7A2B45818DBD6E44 CRC64;
     MAPWLQLCSV FFTVNACLNG SQLAVAAGGS GRARGADTCG WRGVGPASRN SGLYNITFKY
     DNCTTYLNPV GKHVIADAQN ITISQYACHD QVAVTILWSP GALGIEFLKG FRVILEELKS
     EGRQCQQLIL KDPKQLNSSF KRTGMESQPF LNMKFETDYF VKVVPFPSIK NESNYHPFFF
     RTRACDLLLQ PDNLACKPFW KPRNLNISQH GSDMQVSFDH APHNFGFRFF YLHYKLKHEG
     PFKRKTCKQE QTTETTSCLL QNVSPGDYII ELVDDTNTTR KVMHYALKPV HSPWAGPIRA
     VAITVPLVVI SAFATLFTVM CRKKQQENIY SHLDEESSES STYTAALPRE RLRPRPKVFL
     CYSSKDGQNH MNVVQCFAYF LQDFCGCEVA LDLWEDFSLC REGQREWVIQ KIHESQFIIV
     VCSKGMKYFV DKKNYKHKGG GRGSGKGELF LVAVSAIAEK LRQAKQSSSA ALSKFIAVYF
     DYSCEGDVPG ILDLSTKYRL MDNLPQLCSH LHSRDHGLQE PGQHTRQGSR RNYFRSKSGR
     SLYVAICNMH QFIDEEPDWF EKQFVPFHPP PLRYREPVLE KFDSGLVLND VMCKPGPESD
     FCLKVEAAVL GATGPADSQH ESQHGGLDQD GEARPALDGS AALQPLLHTV KAGSPSDMPR
     DSGIYDSSVP SSELSLPLME GLSTDQTETS SLTESVSSSS GLGEEEPPAL PSKLLSSGSC
     KADLGCRSYT DELHAVAPL
 
 
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