RHDF1_HUMAN
ID RHDF1_HUMAN Reviewed; 855 AA.
AC Q96CC6; Q04842; Q1W6H2; Q4TT59; Q96S34; Q9H6E1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Inactive rhomboid protein 1;
DE Short=iRhom1;
DE AltName: Full=Epidermal growth factor receptor-related protein;
DE AltName: Full=Rhomboid 5 homolog 1;
DE AltName: Full=Rhomboid family member 1;
DE AltName: Full=p100hRho;
GN Name=RHBDF1; Synonyms=C16orf8, DIST1, IRHOM1;
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].
RX PubMed=16728641; DOI=10.1126/science.1126431;
RA De Gobbi M., Viprakasit V., Hughes J.R., Fisher C., Buckle V.J., Ayyub H.,
RA Gibbons R.J., Vernimmen D., Yoshinaga Y., de Jong P., Cheng J.-F.,
RA Rubin E.M., Wood W.G., Bowden D., Higgs D.R.;
RT "A regulatory SNP causes a human genetic disease by creating a new
RT transcriptional promoter.";
RL Science 312:1215-1217(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 510-669, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8318735; DOI=10.1007/bf00357090;
RA Kielman M.F., Smits R., Devi T.S., Fodde R., Bernini L.F.;
RT "Homology of a 130-kb region enclosing the alpha-globin gene cluster, the
RT alpha-locus controlling region, and two non-globin genes in human and
RT mouse.";
RL Mamm. Genome 4:314-323(1993).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TGFA AND HBEGF,
RP GLYCOSYLATION AT ASN-583, MUTAGENESIS OF ASN-131; ASN-381 AND ASN-583, AND
RP TISSUE SPECIFICITY.
RX PubMed=15965977; DOI=10.1002/dvdy.20450;
RA Nakagawa T., Guichard A., Castro C.P., Xiao Y., Rizen M., Zhang H.-Z.,
RA Hu D., Bang A., Helms J., Bier E., Derynck R.;
RT "Characterization of a human rhomboid homolog, p100hRho/RHBDF1, which
RT interacts with TGF-alpha family ligands.";
RL Dev. Dyn. 233:1315-1331(2005).
RN [9]
RP FUNCTION.
RX PubMed=18524845; DOI=10.1158/1535-7163.mct-08-0104;
RA Yan Z., Zou H., Tian F., Grandis J.R., Mixson A.J., Lu P.Y., Li L.Y.;
RT "Human rhomboid family-1 gene silencing causes apoptosis or autophagy to
RT epithelial cancer cells and inhibits xenograft tumor growth.";
RL Mol. Cancer Ther. 7:1355-1364(2008).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18832597; DOI=10.1096/fj.08-112771;
RA Zou H., Thomas S.M., Yan Z.W., Grandis J.R., Vogt A., Li L.Y.;
RT "Human rhomboid family-1 gene RHBDF1 participates in GPCR-mediated
RT transactivation of EGFR growth signals in head and neck squamous cancer
RT cells.";
RL FASEB J. 23:425-432(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EGF.
RX PubMed=21439629; DOI=10.1016/j.cell.2011.02.047;
RA Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.;
RT "Rhomboid family pseudoproteases use the ER quality control machinery to
RT regulate intercellular signaling.";
RL Cell 145:79-91(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-390, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [13]
RP INTERACTION WITH ADAM17 AND FRMD8.
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 [14]
RP INTERACTION WITH 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. {ECO:0000269|PubMed:15965977,
CC ECO:0000269|PubMed:18524845, ECO:0000269|PubMed:18832597,
CC ECO:0000269|PubMed:21439629}.
CC -!- SUBUNIT: Homodimer, or homooligomer. Interacts with TGFA and HBEGF
CC (PubMed:15965977). Interacts with EGF; may retain EGF in the
CC endoplasmic reticulum and regulates its degradation through the
CC endoplasmic reticulum-associated degradation (ERAD) (PubMed:21439629).
CC Interacts (via cytoplasmic N-terminus) with FRMD8/iTAP; this
CC interaction leads to mutual protein stabilization (PubMed:29897333,
CC PubMed:29897336). Interacts with ADAM17/TACE (PubMed:29897333).
CC {ECO:0000269|PubMed:15965977, ECO:0000269|PubMed:21439629,
CC ECO:0000269|PubMed:29897333, ECO:0000269|PubMed:29897336}.
CC -!- INTERACTION:
CC Q96CC6; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-3865223, EBI-12039345;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15965977, ECO:0000269|PubMed:18832597,
CC ECO:0000269|PubMed:21439629}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:15965977,
CC ECO:0000269|PubMed:18832597}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Predominantly localized in the endoplasmic
CC reticulum membrane (PubMed:15965977). {ECO:0000269|PubMed:15965977}.
CC -!- TISSUE SPECIFICITY: Highly expressed in cerebellum, cerebrum, heart,
CC skeletal muscle, placenta, pancreatic islet and testis. Detected at
CC lower levels in colon, kidney, small intestine and lung.
CC {ECO:0000269|PubMed:15965977, ECO:0000269|PubMed:8318735}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15965977}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA02490.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK61212.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABD95905.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAW85873.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ431198; ABD95905.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK026010; BAB15318.1; -; mRNA.
DR EMBL; AK291177; BAF83866.1; -; mRNA.
DR EMBL; AE006462; AAK61212.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z69719; CAI95608.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85873.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471112; EAW85876.1; -; Genomic_DNA.
DR EMBL; BC014425; AAH14425.1; -; mRNA.
DR EMBL; M99624; AAA02490.1; ALT_INIT; mRNA.
DR CCDS; CCDS32344.1; -.
DR RefSeq; NP_071895.3; NM_022450.3.
DR RefSeq; XP_005255551.1; XM_005255494.1.
DR AlphaFoldDB; Q96CC6; -.
DR BioGRID; 122129; 9.
DR ELM; Q96CC6; -.
DR IntAct; Q96CC6; 4.
DR STRING; 9606.ENSP00000262316; -.
DR MEROPS; S54.952; -.
DR GlyGen; Q96CC6; 1 site.
DR iPTMnet; Q96CC6; -.
DR PhosphoSitePlus; Q96CC6; -.
DR SwissPalm; Q96CC6; -.
DR BioMuta; RHBDF1; -.
DR DMDM; 190360226; -.
DR EPD; Q96CC6; -.
DR jPOST; Q96CC6; -.
DR MassIVE; Q96CC6; -.
DR MaxQB; Q96CC6; -.
DR PaxDb; Q96CC6; -.
DR PeptideAtlas; Q96CC6; -.
DR PRIDE; Q96CC6; -.
DR ProteomicsDB; 76178; -.
DR Antibodypedia; 22449; 38 antibodies from 13 providers.
DR DNASU; 64285; -.
DR Ensembl; ENST00000262316.10; ENSP00000262316.5; ENSG00000007384.15.
DR GeneID; 64285; -.
DR KEGG; hsa:64285; -.
DR MANE-Select; ENST00000262316.10; ENSP00000262316.5; NM_022450.5; NP_071895.3.
DR UCSC; uc002cfl.4; human.
DR CTD; 64285; -.
DR DisGeNET; 64285; -.
DR GeneCards; RHBDF1; -.
DR HGNC; HGNC:20561; RHBDF1.
DR HPA; ENSG00000007384; Low tissue specificity.
DR MIM; 614403; gene.
DR neXtProt; NX_Q96CC6; -.
DR OpenTargets; ENSG00000007384; -.
DR PharmGKB; PA25563; -.
DR VEuPathDB; HostDB:ENSG00000007384; -.
DR eggNOG; KOG2290; Eukaryota.
DR GeneTree; ENSGT00940000156278; -.
DR HOGENOM; CLU_011531_1_1_1; -.
DR InParanoid; Q96CC6; -.
DR OMA; GGTENMA; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; Q96CC6; -.
DR TreeFam; TF312988; -.
DR PathwayCommons; Q96CC6; -.
DR SignaLink; Q96CC6; -.
DR BioGRID-ORCS; 64285; 30 hits in 1077 CRISPR screens.
DR ChiTaRS; RHBDF1; human.
DR GeneWiki; RHBDF1; -.
DR GenomeRNAi; 64285; -.
DR Pharos; Q96CC6; Tbio.
DR PRO; PR:Q96CC6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96CC6; protein.
DR Bgee; ENSG00000007384; Expressed in tibial nerve and 182 other tissues.
DR ExpressionAtlas; Q96CC6; baseline and differential.
DR Genevisible; Q96CC6; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; IMP:UniProtKB.
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 Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Growth factor binding; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..855
FT /note="Inactive rhomboid protein 1"
FT /id="PRO_0000340104"
FT TOPO_DOM 1..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..655
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..714
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..772
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..803
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 825..855
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIX5"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIX5"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIX5"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15965977"
FT VARIANT 265
FT /note="R -> W (in dbSNP:rs3213511)"
FT /id="VAR_044006"
FT MUTAGEN 131
FT /note="N->Q: No effect."
FT /evidence="ECO:0000269|PubMed:15965977"
FT MUTAGEN 381
FT /note="N->Q: No effect."
FT /evidence="ECO:0000269|PubMed:15965977"
FT MUTAGEN 583
FT /note="N->Q: Loss of N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15965977"
FT CONFLICT 5
FT /note="R -> C (in Ref. 1; ABD95905)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Q -> R (in Ref. 6; AAH14425)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="T -> A (in Ref. 2; BAB15318)"
FT /evidence="ECO:0000305"
FT CONFLICT 551..553
FT /note="DPR -> GSQ (in Ref. 7; AAA02490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 855 AA; 97401 MW; C39FCCE4CE89323B CRC64;
MSEARRDSTS SLQRKKPPWL KLDIPSAVPL TAEEPSFLQP LRRQAFLRSV SMPAETAHIS
SPHHELRRPV LQRQTSITQT IRRGTADWFG VSKDSDSTQK WQRKSIRHCS QRYGKLKPQV
LRELDLPSQD NVSLTSTETP PPLYVGPCQL GMQKIIDPLA RGRAFRVADD TAEGLSAPHT
PVTPGAASLC SFSSSRSGFH RLPRRRKRES VAKMSFRAAA ALMKGRSVRD GTFRRAQRRS
FTPASFLEED TTDFPDELDT SFFAREGILH EELSTYPDEV FESPSEAALK DWEKAPEQAD
LTGGALDRSE LERSHLMLPL ERGWRKQKEG AAAPQPKVRL RQEVVSTAGP RRGQRIAVPV
RKLFAREKRP YGLGMVGRLT NRTYRKRIDS FVKRQIEDMD DHRPFFTYWL TFVHSLVTIL
AVCIYGIAPV GFSQHETVDS VLRNRGVYEN VKYVQQENFW IGPSSEALIH LGAKFSPCMR
QDPQVHSFIR SAREREKHSA CCVRNDRSGC VQTSEEECSS TLAVWVKWPI HPSAPELAGH
KRQFGSVCHQ DPRVCDEPSS EDPHEWPEDI TKWPICTKNS AGNHTNHPHM DCVITGRPCC
IGTKGRCEIT SREYCDFMRG YFHEEATLCS QVHCMDDVCG LLPFLNPEVP DQFYRLWLSL
FLHAGILHCL VSICFQMTVL RDLEKLAGWH RIAIIYLLSG VTGNLASAIF LPYRAEVGPA
GSQFGILACL FVELFQSWQI LARPWRAFFK LLAVVLFLFT FGLLPWIDNF AHISGFISGL
FLSFAFLPYI SFGKFDLYRK RCQIIIFQVV FLGLLAGLVV LFYVYPVRCE WCEFLTCIPF
TDKFCEKYEL DAQLH
