RHDF2_HUMAN
ID RHDF2_HUMAN Reviewed; 856 AA.
AC Q6PJF5; A6NEM3; A8K801; Q5U607; Q5YGQ8; Q9H6E9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Inactive rhomboid protein 2;
DE Short=iRhom2;
DE AltName: Full=Rhomboid 5 homolog 2;
DE AltName: Full=Rhomboid family member 2;
DE AltName: Full=Rhomboid veinlet-like protein 5;
DE AltName: Full=Rhomboid veinlet-like protein 6;
GN Name=RHBDF2; Synonyms=IRHOM2, RHBDL5, RHBDL6;
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 2), AND VARIANT LEU-208.
RC TISSUE=Liver;
RA Kong X., Teng X., Hu L.;
RT "Molecular cloning of human RHBDL5.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LEU-208.
RC TISSUE=Kidney epithelium, Spleen, and Synovium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-208.
RC TISSUE=Eye, and Uterus;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-325 AND SER-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANTS TOC THR-186 AND
RP LEU-189.
RX PubMed=22265016; DOI=10.1016/j.ajhg.2011.12.008;
RA Blaydon D.C., Etheridge S.L., Risk J.M., Hennies H.C., Gay L.J.,
RA Carroll R., Plagnol V., McRonald F.E., Stevens H.P., Spurr N.K.,
RA Bishop D.T., Ellis A., Jankowski J., Field J.K., Leigh I.M., South A.P.,
RA Kelsell D.P.;
RT "RHBDF2 mutations are associated with tylosis, a familial esophageal cancer
RT syndrome.";
RL Am. J. Hum. Genet. 90:340-346(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-113; SER-325 AND
RP SER-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP INTERACTION WITH ADAM17 AND FRMD8, AND SUBCELLULAR LOCATION.
RX PubMed=29897333; DOI=10.7554/elife.35032;
RA Oikonomidi I., Burbridge E., Cavadas M., Sullivan G., Collis B.,
RA Naegele H., Clancy D., Brezinova J., Hu T., Bileck A., Gerner C.,
RA Bolado A., von Kriegsheim A., Martin S.J., Steinberg F., Strisovsky K.,
RA Adrain C.;
RT "iTAP, a novel iRhom interactor, controls TNF secretion by policing the
RT stability of iRhom/TACE.";
RL Elife 7:0-0(2018).
RN [11]
RP INTERACTION WITH ADAM17 AND FRMD8.
RX PubMed=29897336; DOI=10.7554/elife.35012;
RA Kuenzel U., Grieve A.G., Meng Y., Sieber B., Cowley S.A., Freeman M.;
RT "FRMD8 promotes inflammatory and growth factor signalling by stabilising
RT the iRhom/ADAM17 sheddase complex.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Regulates ADAM17 protease, a sheddase of the epidermal growth
CC factor (EGF) receptor ligands and TNF, thereby plays a role in sleep,
CC cell survival, proliferation, migration and inflammation. Does not
CC exhibit any protease activity on its own.
CC {ECO:0000250|UniProtKB:Q80WQ6}.
CC -!- SUBUNIT: Interacts with EGF (By similarity). Interacts (via cytoplasmic
CC N-terminus) with FRMD8/iTAP; this interaction leads to mutual protein
CC stabilization (PubMed:29897333, PubMed:29897336). Interacts with
CC ADAM17/TACE (PubMed:29897333, PubMed:29897336).
CC {ECO:0000250|UniProtKB:Q80WQ6, ECO:0000269|PubMed:29897333,
CC ECO:0000269|PubMed:29897336}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q80WQ6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q80WQ6}. Cell membrane
CC {ECO:0000269|PubMed:22265016, ECO:0000269|PubMed:29897333}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PJF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PJF5-2; Sequence=VSP_034368;
CC -!- TISSUE SPECIFICITY: Found in the epidermis and esophageal epithelium.
CC {ECO:0000269|PubMed:22265016}.
CC -!- DISEASE: Tylosis with esophageal cancer (TOC) [MIM:148500]: An
CC autosomal dominant syndrome characterized by diffuse palmoplantar
CC keratoderma, oral leukokeratosis, and a high lifetime risk of
CC esophageal cancer. {ECO:0000269|PubMed:22265016}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35829.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15310.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY500247; AAS77567.1; -; mRNA.
DR EMBL; AK025994; BAB15310.1; ALT_INIT; mRNA.
DR EMBL; AK292135; BAF84824.1; -; mRNA.
DR EMBL; AK292166; BAF84855.1; -; mRNA.
DR EMBL; AC015802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035829; AAH35829.1; ALT_INIT; mRNA.
DR EMBL; BC016034; AAH16034.2; -; mRNA.
DR CCDS; CCDS32743.1; -. [Q6PJF5-1]
DR CCDS; CCDS32744.1; -. [Q6PJF5-2]
DR RefSeq; NP_001005498.2; NM_001005498.3. [Q6PJF5-2]
DR RefSeq; NP_078875.4; NM_024599.5. [Q6PJF5-1]
DR RefSeq; XP_005257726.1; XM_005257669.3. [Q6PJF5-1]
DR RefSeq; XP_005257727.1; XM_005257670.1.
DR RefSeq; XP_011523551.1; XM_011525249.2. [Q6PJF5-2]
DR RefSeq; XP_011523552.1; XM_011525250.2. [Q6PJF5-2]
DR RefSeq; XP_011523553.1; XM_011525251.2. [Q6PJF5-2]
DR RefSeq; XP_016880568.1; XM_017025079.1.
DR AlphaFoldDB; Q6PJF5; -.
DR BioGRID; 122779; 200.
DR ELM; Q6PJF5; -.
DR IntAct; Q6PJF5; 11.
DR STRING; 9606.ENSP00000322775; -.
DR MEROPS; S54.953; -.
DR GlyGen; Q6PJF5; 1 site.
DR iPTMnet; Q6PJF5; -.
DR PhosphoSitePlus; Q6PJF5; -.
DR BioMuta; RHBDF2; -.
DR DMDM; 193806488; -.
DR EPD; Q6PJF5; -.
DR jPOST; Q6PJF5; -.
DR MassIVE; Q6PJF5; -.
DR MaxQB; Q6PJF5; -.
DR PaxDb; Q6PJF5; -.
DR PeptideAtlas; Q6PJF5; -.
DR PRIDE; Q6PJF5; -.
DR ProteomicsDB; 67199; -. [Q6PJF5-1]
DR ProteomicsDB; 67200; -. [Q6PJF5-2]
DR Antibodypedia; 19692; 81 antibodies from 21 providers.
DR DNASU; 79651; -.
DR Ensembl; ENST00000313080.8; ENSP00000322775.3; ENSG00000129667.13. [Q6PJF5-1]
DR Ensembl; ENST00000591885.5; ENSP00000466867.1; ENSG00000129667.13. [Q6PJF5-2]
DR Ensembl; ENST00000675367.1; ENSP00000501790.1; ENSG00000129667.13. [Q6PJF5-2]
DR GeneID; 79651; -.
DR KEGG; hsa:79651; -.
DR MANE-Select; ENST00000675367.1; ENSP00000501790.1; NM_001005498.4; NP_001005498.2. [Q6PJF5-2]
DR UCSC; uc002jrq.3; human. [Q6PJF5-1]
DR CTD; 79651; -.
DR DisGeNET; 79651; -.
DR GeneCards; RHBDF2; -.
DR HGNC; HGNC:20788; RHBDF2.
DR HPA; ENSG00000129667; Low tissue specificity.
DR MalaCards; RHBDF2; -.
DR MIM; 148500; phenotype.
DR MIM; 614404; gene.
DR neXtProt; NX_Q6PJF5; -.
DR OpenTargets; ENSG00000129667; -.
DR Orphanet; 2198; Palmoplantar keratoderma-esophageal carcinoma syndrome.
DR PharmGKB; PA134980674; -.
DR VEuPathDB; HostDB:ENSG00000129667; -.
DR eggNOG; KOG2290; Eukaryota.
DR GeneTree; ENSGT00940000159027; -.
DR HOGENOM; CLU_011531_1_1_1; -.
DR InParanoid; Q6PJF5; -.
DR OMA; IKRSFAY; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; Q6PJF5; -.
DR TreeFam; TF312988; -.
DR PathwayCommons; Q6PJF5; -.
DR Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response.
DR SignaLink; Q6PJF5; -.
DR BioGRID-ORCS; 79651; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; RHBDF2; human.
DR GeneWiki; RHBDF2; -.
DR GenomeRNAi; 79651; -.
DR Pharos; Q6PJF5; Tbio.
DR PRO; PR:Q6PJF5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6PJF5; protein.
DR Bgee; ENSG00000129667; Expressed in granulocyte and 158 other tissues.
DR ExpressionAtlas; Q6PJF5; baseline and differential.
DR Genevisible; Q6PJF5; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0140318; F:protein transporter activity; TAS:Reactome.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; TAS:Reactome.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1904683; P:regulation of metalloendopeptidase activity; IEA:Ensembl.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR022241; Rhomboid_SP.
DR Pfam; PF01694; Rhomboid; 1.
DR Pfam; PF12595; Rhomboid_SP; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant;
KW Endoplasmic reticulum; Growth factor binding; Membrane;
KW Palmoplantar keratoderma; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..856
FT /note="Inactive rhomboid protein 2"
FT /id="PRO_0000341938"
FT TOPO_DOM 1..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..660
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..715
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..773
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..856
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..271
FT /note="Involved in interaction with FRMD8"
FT /evidence="ECO:0000269|PubMed:29897333"
FT REGION 531..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80WQ6"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80WQ6"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 51..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_034368"
FT VARIANT 186
FT /note="I -> T (in TOC; dbSNP:rs387907129)"
FT /evidence="ECO:0000269|PubMed:22265016"
FT /id="VAR_067827"
FT VARIANT 189
FT /note="P -> L (in TOC; dbSNP:rs387907130)"
FT /evidence="ECO:0000269|PubMed:22265016"
FT /id="VAR_067828"
FT VARIANT 208
FT /note="P -> L (in dbSNP:rs3744045)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_044125"
FT VARIANT 249
FT /note="A -> T (in dbSNP:rs34814954)"
FT /id="VAR_044126"
FT VARIANT 528
FT /note="D -> Y (in dbSNP:rs11553545)"
FT /id="VAR_044127"
FT CONFLICT 67
FT /note="A -> S (in Ref. 2; BAF84824 and 4; AAH16034)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="N -> D (in Ref. 2; BAF84855)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="D -> G (in Ref. 2; BAF84855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 856 AA; 96686 MW; 69C40A21EBDBDDC0 CRC64;
MASADKNGGS VSSVSSSRLQ SRKPPNLSIT IPPPEKETQA PGEQDSMLPE GFQNRRLKKS
QPRTWAAHTT ACPPSFLPKR KNPAYLKSVS LQEPRSRWQE SSEKRPGFRR QASLSQSIRK
GAAQWFGVSG DWEGQRQQWQ RRSLHHCSMR YGRLKASCQR DLELPSQEAP SFQGTESPKP
CKMPKIVDPL ARGRAFRHPE EMDRPHAPHP PLTPGVLSLT SFTSVRSGYS HLPRRKRMSV
AHMSLQAAAA LLKGRSVLDA TGQRCRVVKR SFAFPSFLEE DVVDGADTFD SSFFSKEEMS
SMPDDVFESP PLSASYFRGI PHSASPVSPD GVQIPLKEYG RAPVPGPRRG KRIASKVKHF
AFDRKKRHYG LGVVGNWLNR SYRRSISSTV QRQLESFDSH RPYFTYWLTF VHVIITLLVI
CTYGIAPVGF AQHVTTQLVL RNKGVYESVK YIQQENFWVG PSSIDLIHLG AKFSPCIRKD
GQIEQLVLRE RDLERDSGCC VQNDHSGCIQ TQRKDCSETL ATFVKWQDDT GPPMDKSDLG
QKRTSGAVCH QDPRTCEEPA SSGAHIWPDD ITKWPICTEQ ARSNHTGFLH MDCEIKGRPC
CIGTKGSCEI TTREYCEFMH GYFHEEATLC SQVHCLDKVC GLLPFLNPEV PDQFYRLWLS
LFLHAGVVHC LVSVVFQMTI LRDLEKLAGW HRIAIIFILS GITGNLASAI FLPYRAEVGP
AGSQFGLLAC LFVELFQSWP LLERPWKAFL NLSAIVLFLF ICGLLPWIDN IAHIFGFLSG
LLLAFAFLPY ITFGTSDKYR KRALILVSLL AFAGLFAALV LWLYIYPINW PWIEHLTCFP
FTSRFCEKYE LDQVLH