ID   TRI10_HUMAN             Reviewed;         481 AA.
AC   Q9UDY6; A6NF84; Q5SRJ5; Q5SRK8; Q86Z08; Q96QB6; Q9C023; Q9C024;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 3.
DT   24-JAN-2024, entry version 206.
DE   RecName: Full=Tripartite motif-containing protein 10;
DE   AltName: Full=B30-RING finger protein;
DE   AltName: Full=RING finger protein 9;
GN   Name=TRIM10; Synonyms=RFB30, RNF9;
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 [GENOMIC DNA] (ISOFORM ALPHA).
RC   TISSUE=Testis;
RX   PubMed=9271628; DOI=10.1007/s002510050292;
RA   Henry J., Ribouchon M.-T., Depetris D., Mattei M.-G., Offer C.,
RA   Tazi-Ahnini R., Pontarotti P.;
RT   "Cloning, structural analysis, and mapping of the B30 and B7 multigenic
RT   families to the major histocompatibility complex (MHC) and other
RT   chromosomal regions.";
RL   Immunogenetics 46:383-395(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA   Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA   Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA   Pelicci P.G., Ballabio A.;
RT   "The tripartite motif family identifies cell compartments.";
RL   EMBO J. 20:2140-2151(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Peripheral blood leukocyte;
RX   PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA   Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA   Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA   Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA   Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA   Inoko H., Bahram S.;
RT   "Rapid evolution of major histocompatibility complex class I genes in
RT   primates generates new disease alleles in humans via hitchhiking
RT   diversity.";
RL   Genetics 173:1555-1570(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shiina S., Tamiya G., Oka A., Inoko H.;
RT   "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT   "Genome diversity in HLA: a new strategy for detection of genetic
RT   polymorphisms in expressed genes within the HLA class III and class I
RT   regions.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 BETA).
RC   TISSUE=Liver;
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   FUNCTION, INTERACTION WITH IFNAR1, AND SUBCELLULAR LOCATION.
RX   PubMed=33811647; DOI=10.1002/eji.202049073;
RA   Guo M., Cao W., Chen S., Tian R., Wang L., Liu Q., Zhang L., Wang Z.,
RA   Zhao M., Lu Q., Zhu H.;
RT   "TRIM10 binds to IFN-alpha/beta receptor 1 to negatively regulate type I
RT   IFN signal transduction.";
RL   Eur. J. Immunol. 51:1762-1773(2021).
CC   -!- FUNCTION: E3 ligase that plays an essential role in the differentiation
CC       and survival of terminal erythroid cells. May directly bind to PTEN and
CC       promote its ubiquitination, resulting in its proteasomal degradation
CC       and activation of hypertrophic signaling (By similarity). In addition,
CC       plays a role in immune response regulation by repressing the
CC       phosphorylation of STAT1 and STAT2 in the interferon/JAK/STAT signaling
CC       pathway independent of its E3 ligase activity. Mechanistically,
CC       interacts with the intracellular domain of IFNAR1 and thereby inhibits
CC       the association between TYK2 and IFNAR1 (PubMed:33811647).
CC       {ECO:0000250|UniProtKB:Q9WUH5, ECO:0000269|PubMed:33811647}.
CC   -!- SUBUNIT: Interacts with IFNAR1; this interaction prevents association
CC       of IFNAR1 with TYK2. {ECO:0000269|PubMed:33811647}.
CC   -!- INTERACTION:
CC       Q9UDY6; P25786: PSMA1; NbExp=4; IntAct=EBI-6427325, EBI-359352;
CC       Q9UDY6; Q5W5X9: TTC23; NbExp=4; IntAct=EBI-6427325, EBI-6447954;
CC       Q9UDY6; Q9UQR1: ZNF148; NbExp=3; IntAct=EBI-6427325, EBI-2688184;
CC       Q9UDY6-2; P55040: GEM; NbExp=3; IntAct=EBI-11981577, EBI-744104;
CC       Q9UDY6-2; O14964: HGS; NbExp=3; IntAct=EBI-11981577, EBI-740220;
CC       Q9UDY6-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11981577, EBI-739832;
CC       Q9UDY6-2; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-11981577, EBI-748391;
CC       Q9UDY6-2; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-11981577, EBI-17716262;
CC       Q9UDY6-2; Q96DX7: TRIM44; NbExp=4; IntAct=EBI-11981577, EBI-8787399;
CC       Q9UDY6-2; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-11981577, EBI-744257;
CC       Q9UDY6-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-11981577, EBI-4395669;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331580,
CC       ECO:0000269|PubMed:33811647}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha;
CC         IsoId=Q9UDY6-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=Q9UDY6-2; Sequence=VSP_005748;
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; Y07829; CAB52384.1; -; Genomic_DNA.
DR   EMBL; AF220122; AAG53495.1; -; mRNA.
DR   EMBL; AF220123; AAG53496.1; -; mRNA.
DR   EMBL; AB202085; BAE78605.1; -; Genomic_DNA.
DR   EMBL; AB103595; BAF31256.1; -; Genomic_DNA.
DR   EMBL; BA000025; BAB63332.1; -; Genomic_DNA.
DR   EMBL; AB088089; BAC54921.1; -; Genomic_DNA.
DR   EMBL; AL669914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL671859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL844220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX005441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX927221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR753815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR788282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03268.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03269.1; -; Genomic_DNA.
DR   EMBL; BC093926; AAH93926.1; -; mRNA.
DR   EMBL; BC113419; AAI13420.1; -; mRNA.
DR   CCDS; CCDS34375.1; -. [Q9UDY6-1]
DR   CCDS; CCDS4676.1; -. [Q9UDY6-2]
DR   RefSeq; NP_006769.2; NM_006778.3. [Q9UDY6-1]
DR   RefSeq; NP_439893.2; NM_052828.2. [Q9UDY6-2]
DR   PDB; 7QS0; X-ray; 2.30 A; A/B/C=304-481.
DR   PDBsum; 7QS0; -.
DR   AlphaFoldDB; Q9UDY6; -.
DR   SMR; Q9UDY6; -.
DR   BioGRID; 115413; 52.
DR   IntAct; Q9UDY6; 24.
DR   STRING; 9606.ENSP00000397073; -.
DR   PhosphoSitePlus; Q9UDY6; -.
DR   BioMuta; TRIM10; -.
DR   DMDM; 50403805; -.
DR   EPD; Q9UDY6; -.
DR   jPOST; Q9UDY6; -.
DR   MassIVE; Q9UDY6; -.
DR   PaxDb; 9606-ENSP00000397073; -.
DR   PeptideAtlas; Q9UDY6; -.
DR   ProteomicsDB; 84134; -. [Q9UDY6-1]
DR   ProteomicsDB; 84135; -. [Q9UDY6-2]
DR   Antibodypedia; 26232; 191 antibodies from 19 providers.
DR   DNASU; 10107; -.
DR   Ensembl; ENST00000259941.6; ENSP00000259941.6; ENSG00000137394.14. [Q9UDY6-2]
DR   Ensembl; ENST00000354038.10; ENSP00000343695.6; ENSG00000137394.14. [Q9UDY6-1]
DR   Ensembl; ENST00000376704.3; ENSP00000365894.3; ENSG00000204613.11. [Q9UDY6-2]
DR   Ensembl; ENST00000413055.2; ENSP00000393787.2; ENSG00000227472.8. [Q9UDY6-2]
DR   Ensembl; ENST00000416714.2; ENSP00000405578.2; ENSG00000229381.8. [Q9UDY6-2]
DR   Ensembl; ENST00000417411.6; ENSP00000393576.2; ENSG00000237192.8. [Q9UDY6-2]
DR   Ensembl; ENST00000426996.6; ENSP00000397440.2; ENSG00000227472.8. [Q9UDY6-1]
DR   Ensembl; ENST00000428611.6; ENSP00000412370.2; ENSG00000229346.8. [Q9UDY6-2]
DR   Ensembl; ENST00000431258.6; ENSP00000395598.2; ENSG00000235025.8. [Q9UDY6-1]
DR   Ensembl; ENST00000446013.2; ENSP00000398404.2; ENSG00000237703.8. [Q9UDY6-2]
DR   Ensembl; ENST00000447465.2; ENSP00000393976.2; ENSG00000235025.8. [Q9UDY6-2]
DR   Ensembl; ENST00000448645.2; ENSP00000399446.2; ENSG00000229346.8. [Q9UDY6-1]
DR   Ensembl; ENST00000449208.6; ENSP00000390497.2; ENSG00000237703.8. [Q9UDY6-1]
DR   Ensembl; ENST00000449742.7; ENSP00000397073.2; ENSG00000204613.11. [Q9UDY6-1]
DR   Ensembl; ENST00000451727.2; ENSP00000391445.2; ENSG00000237192.8. [Q9UDY6-1]
DR   Ensembl; ENST00000456988.6; ENSP00000410849.2; ENSG00000229381.8. [Q9UDY6-1]
DR   GeneID; 10107; -.
DR   KEGG; hsa:10107; -.
DR   MANE-Select; ENST00000449742.7; ENSP00000397073.2; NM_006778.4; NP_006769.2.
DR   UCSC; uc003npn.3; human. [Q9UDY6-1]
DR   AGR; HGNC:10072; -.
DR   CTD; 10107; -.
DR   DisGeNET; 10107; -.
DR   GeneCards; TRIM10; -.
DR   HGNC; HGNC:10072; TRIM10.
DR   HPA; ENSG00000204613; Tissue enhanced (bone marrow, kidney, liver).
DR   MIM; 605701; gene.
DR   neXtProt; NX_Q9UDY6; -.
DR   OpenTargets; ENSG00000204613; -.
DR   PharmGKB; PA35536; -.
DR   VEuPathDB; HostDB:ENSG00000204613; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000161525; -.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   InParanoid; Q9UDY6; -.
DR   OMA; SCTMGVV; -.
DR   OrthoDB; 3453019at2759; -.
DR   PhylomeDB; Q9UDY6; -.
DR   TreeFam; TF342569; -.
DR   PathwayCommons; Q9UDY6; -.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   SignaLink; Q9UDY6; -.
DR   SIGNOR; Q9UDY6; -.
DR   BioGRID-ORCS; 10107; 11 hits in 1185 CRISPR screens.
DR   ChiTaRS; TRIM10; human.
DR   GenomeRNAi; 10107; -.
DR   Pharos; Q9UDY6; Tbio.
DR   PRO; PR:Q9UDY6; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9UDY6; Protein.
DR   Bgee; ENSG00000137394; Expressed in liver.
DR   ExpressionAtlas; Q9UDY6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd16593; RING-HC_TRIM10_C-IV; 1.
DR   CDD; cd15827; SPRY_PRY_TRIM10; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR042784; TRIM10_RING-HC.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF329; TRIPARTITE MOTIF-CONTAINING PROTEIN 10; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q9UDY6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..481
FT                   /note="Tripartite motif-containing protein 10"
FT                   /id="PRO_0000056211"
FT   DOMAIN          292..481
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         16..61
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         94..135
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          150..177
FT                   /evidence="ECO:0000255"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   VAR_SEQ         369..481
FT                   /note="VSIDLAHGGSCTVGVVSEDVQRKGELRLRPEEGVWAVRLAWGFVSALGSFPT
FT                   RLTLKEQPRQVRVSLDYEVGWVTFTNAVTREPIYTFTASFTRKVIPFFGLWGRGSSFSL
FT                   SS -> WMARVPGDSGCCQFCSPPSVLGTEVAA (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:11331580,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_005748"
FT   VARIANT         65
FT                   /note="R -> H (in dbSNP:rs12212092)"
FT                   /id="VAR_052127"
FT   VARIANT         119
FT                   /note="V -> M (in dbSNP:rs17194446)"
FT                   /id="VAR_052128"
FT   CONFLICT        104
FT                   /note="E -> G (in Ref. 1; CAB52384)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="E -> SR (in Ref. 2; AAG53495/AAG53496)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="E -> K (in Ref. 2; AAG53495/AAG53496)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336
FT                   /note="Y -> S (in Ref. 1; CAB52384 and 2; AAG53495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377
FT                   /note="G -> A (in Ref. 1; CAB52384 and 2; AAG53495)"
FT                   /evidence="ECO:0000305"
FT   TURN            316..318
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          329..334
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          349..351
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          353..358
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          362..376
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          378..385
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   HELIX           398..400
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          402..408
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          411..414
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          416..418
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          420..422
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          429..436
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   TURN            437..440
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          441..446
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   TURN            447..449
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          452..457
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          464..472
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   STRAND          475..480
FT                   /evidence="ECO:0007829|PDB:7QS0"
FT   CONFLICT        Q9UDY6-2:379
FT                   /note="C -> G (in Ref. 2; AAG53496)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   481 AA;  55037 MW;  49A1A11F391F5F98 CRC64;
     MASAASVTSL ADEVNCPICQ GTLREPVTID CGHNFCRACL TRYCEIPGPD LEESPTCPLC
     KEPFRPGSFR PNWQLANVVE NIERLQLVST LGLGEEDVCQ EHGEKIYFFC EDDEMQLCVV
     CREAGEHATH TMRFLEDAAA PYREQIHKCL KCLRKEREEI QEIQSRENKR MQVLLTQVST
     KRQQVISEFA HLRKFLEEQQ SILLAQLESQ DGDILRQRDE FDLLVAGEIC RFSALIEELE
     EKNERPAREL LTDIRSTLIR CETRKCRKPV AVSPELGQRI RDFPQQALPL QREMKMFLEK
     LCFELDYEPA HISLDPQTSH PKLLLSEDHQ RAQFSYKWQN SPDNPQRFDR ATCVLAHTGI
     TGGRHTWVVS IDLAHGGSCT VGVVSEDVQR KGELRLRPEE GVWAVRLAWG FVSALGSFPT
     RLTLKEQPRQ VRVSLDYEVG WVTFTNAVTR EPIYTFTASF TRKVIPFFGL WGRGSSFSLS
     S
//