TRI68_HUMAN
ID TRI68_HUMAN Reviewed; 485 AA.
AC Q6AZZ1; A6NI19; A8K551; B3KPM5; B4DVK4; Q8WZ70; Q96LE5; Q96PF7; Q9H9C2;
AC Q9NW18;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM68;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 137;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM68 {ECO:0000305};
DE AltName: Full=SSA protein SS-56;
DE Short=SS-56;
DE AltName: Full=Tripartite motif-containing protein 68;
GN Name=TRIM68; Synonyms=GC109, RNF137, SS56;
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), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, IDENTIFICATION AS AUTOANTIGEN IN AUTOIMMUNE DISEASES, AND VARIANT
RP TYR-442.
RX PubMed=11560955; DOI=10.1172/jci200113469;
RA Billaut-Mulot O., Cocude C., Kolesnitchenko V., Truong M.-J., Chan E.K.L.,
RA Hachulla E., de La Tribonniere X., Capron A., Bahr G.M.;
RT "SS-56, a novel cellular target of autoantibody responses in Sjogren
RT syndrome and systemic lupus erythematosus.";
RL J. Clin. Invest. 108:861-869(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Rhodes D.A., Allcock R.J.N., Trowsdale J.;
RT "Cloning and characterization of FLJ10369, a novel Ro/SSA1-related gene on
RT human chromosome 11p15.5.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Spleen, and Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
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] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-427 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11597395; DOI=10.1016/s0959-8049(01)00259-3;
RA Chang G.T., Steenbeek M., Schippers E., Blok L.J., van Weerden W.M.,
RA van Alewijk D.C., Eussen B.H., van Steenbrugge G.J., Brinkmann A.O.;
RT "A novel gene on human chromosome 2p24 is differentially expressed between
RT androgen-dependent and androgen-independent prostate cancer cells.";
RL Eur. J. Cancer 37:2129-2134(2001).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH KAT5
RP AND AR, DOMAIN RING, AND AUTOUBIQUITINATION.
RX PubMed=18451177; DOI=10.1158/0008-5472.can-07-6059;
RA Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M., Shinohara N.,
RA Nonomura K., Hatakeyama S.;
RT "TRIM68 regulates ligand-dependent transcription of androgen receptor in
RT prostate cancer cells.";
RL Cancer Res. 68:3486-3494(2008).
CC -!- FUNCTION: Functions as a ubiquitin E3 ligase. Acts as a coactivator of
CC androgen receptor (AR) depending on its ubiquitin ligase activity.
CC {ECO:0000269|PubMed:18451177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with AR/androgen receptor (via ligand-binding
CC domain). Interacts with KAT5/TIP60. {ECO:0000269|PubMed:18451177}.
CC -!- INTERACTION:
CC Q6AZZ1; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-2130449, EBI-11988027;
CC Q6AZZ1; Q0VD86: INCA1; NbExp=3; IntAct=EBI-2130449, EBI-6509505;
CC Q6AZZ1; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-2130449, EBI-11953846;
CC Q6AZZ1; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-2130449, EBI-10241252;
CC Q6AZZ1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2130449, EBI-739832;
CC Q6AZZ1; Q9NQ48: LZTFL1; NbExp=3; IntAct=EBI-2130449, EBI-2824799;
CC Q6AZZ1; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-2130449, EBI-2949792;
CC Q6AZZ1; P62487: POLR2G; NbExp=3; IntAct=EBI-2130449, EBI-347928;
CC Q6AZZ1; Q04864-2: REL; NbExp=3; IntAct=EBI-2130449, EBI-10829018;
CC Q6AZZ1; P15884-3: TCF4; NbExp=3; IntAct=EBI-2130449, EBI-13636688;
CC Q6AZZ1; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-2130449, EBI-11139477;
CC Q6AZZ1; Q6AZZ1: TRIM68; NbExp=3; IntAct=EBI-2130449, EBI-2130449;
CC Q6AZZ1; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-2130449, EBI-12287587;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus.
CC Note=Colocalized with AR in nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6AZZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AZZ1-2; Sequence=VSP_055444, VSP_055445;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
CC prostate cancer cell lines. Up-regulation could be restricted to
CC androgen-dependent cells. {ECO:0000269|PubMed:11560955,
CC ECO:0000269|PubMed:11597395, ECO:0000269|PubMed:18451177}.
CC -!- INDUCTION: Up-regulated in prostate cancer.
CC -!- DOMAIN: The RING domain is essential for ubiquitin E3 ligase activity.
CC {ECO:0000269|PubMed:18451177}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:18451177}.
CC -!- MISCELLANEOUS: Antibodies against TRIM68 are found in patients with
CC systemic lupus erythematosus (SLE) and primary Sjoegren syndrome.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91569.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14309.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF360739; AAL11501.1; -; mRNA.
DR EMBL; AF439153; AAL31641.1; -; mRNA.
DR EMBL; AK001231; BAA91569.1; ALT_INIT; mRNA.
DR EMBL; AK022923; BAB14309.1; ALT_INIT; mRNA.
DR EMBL; AK291166; BAF83855.1; -; mRNA.
DR EMBL; AK301120; BAG62716.1; -; mRNA.
DR EMBL; AK056523; BAG51737.1; -; mRNA.
DR EMBL; AC090719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68835.1; -; Genomic_DNA.
DR EMBL; BC075058; AAH75058.1; -; mRNA.
DR EMBL; BC109063; AAI09064.1; -; mRNA.
DR EMBL; AY005802; AAF91075.1; -; mRNA.
DR CCDS; CCDS31356.1; -. [Q6AZZ1-1]
DR RefSeq; NP_001291425.1; NM_001304496.1.
DR RefSeq; NP_060543.5; NM_018073.7. [Q6AZZ1-1]
DR AlphaFoldDB; Q6AZZ1; -.
DR SMR; Q6AZZ1; -.
DR BioGRID; 120434; 101.
DR IntAct; Q6AZZ1; 38.
DR MINT; Q6AZZ1; -.
DR STRING; 9606.ENSP00000300747; -.
DR iPTMnet; Q6AZZ1; -.
DR PhosphoSitePlus; Q6AZZ1; -.
DR BioMuta; TRIM68; -.
DR DMDM; 74748376; -.
DR EPD; Q6AZZ1; -.
DR jPOST; Q6AZZ1; -.
DR MassIVE; Q6AZZ1; -.
DR MaxQB; Q6AZZ1; -.
DR PaxDb; Q6AZZ1; -.
DR PeptideAtlas; Q6AZZ1; -.
DR PRIDE; Q6AZZ1; -.
DR ProteomicsDB; 66204; -. [Q6AZZ1-1]
DR Antibodypedia; 10892; 162 antibodies from 28 providers.
DR DNASU; 55128; -.
DR Ensembl; ENST00000300747.10; ENSP00000300747.5; ENSG00000167333.13. [Q6AZZ1-1]
DR GeneID; 55128; -.
DR KEGG; hsa:55128; -.
DR MANE-Select; ENST00000300747.10; ENSP00000300747.5; NM_018073.8; NP_060543.5.
DR UCSC; uc001lzf.2; human. [Q6AZZ1-1]
DR CTD; 55128; -.
DR DisGeNET; 55128; -.
DR GeneCards; TRIM68; -.
DR HGNC; HGNC:21161; TRIM68.
DR HPA; ENSG00000167333; Low tissue specificity.
DR MIM; 613184; gene.
DR neXtProt; NX_Q6AZZ1; -.
DR OpenTargets; ENSG00000167333; -.
DR PharmGKB; PA134939870; -.
DR VEuPathDB; HostDB:ENSG00000167333; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162047; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q6AZZ1; -.
DR OMA; GNRSEWG; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q6AZZ1; -.
DR TreeFam; TF338674; -.
DR PathwayCommons; Q6AZZ1; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q6AZZ1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55128; 7 hits in 1120 CRISPR screens.
DR ChiTaRS; TRIM68; human.
DR GeneWiki; TRIM68; -.
DR GenomeRNAi; 55128; -.
DR Pharos; Q6AZZ1; Tbio.
DR PRO; PR:Q6AZZ1; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6AZZ1; protein.
DR Bgee; ENSG00000167333; Expressed in palpebral conjunctiva and 175 other tissues.
DR ExpressionAtlas; Q6AZZ1; baseline and differential.
DR Genevisible; Q6AZZ1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR CDD; cd16610; RING-HC_TRIM68_C-IV; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR042656; TRIM68_RING-HC.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 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; SSF49899; SSF49899; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..485
FT /note="E3 ubiquitin-protein ligase TRIM68"
FT /id="PRO_0000249437"
FT DOMAIN 285..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 93..134
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 207..239
FT /evidence="ECO:0000255"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 1..3
FT /note="MDP -> MQK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055444"
FT VAR_SEQ 4..282
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055445"
FT VARIANT 442
FT /note="C -> Y (in dbSNP:rs2231975)"
FT /evidence="ECO:0000269|PubMed:11560955"
FT /id="VAR_027415"
FT VARIANT 457
FT /note="R -> H (in dbSNP:rs2231976)"
FT /id="VAR_063007"
FT VARIANT 466
FT /note="Y -> S (in dbSNP:rs7109316)"
FT /id="VAR_063008"
FT CONFLICT 44
FT /note="W -> R (in Ref. 3; BAG51737)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..114
FT /note="CKEDVL -> RGNSLQ (in Ref. 7; AAF91075)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="I -> V (in Ref. 7; AAF91075)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="A -> G (in Ref. 2; AAL31641)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="D -> V (in Ref. 3; BAG62716)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="S -> P (in Ref. 3; BAB14309)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="K -> Y (in Ref. 7; AAF91075)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="R -> K (in Ref. 7; AAF91075)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="Y -> V (in Ref. 7; AAF91075)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="R -> P (in Ref. 7; AAF91075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 56259 MW; FCB9A6076382E2A5 CRC64;
MDPTALVEAI VEEVACPICM TFLREPMSID CGHSFCHSCL SGLWEIPGES QNWGYTCPLC
RAPVQPRNLR PNWQLANVVE KVRLLRLHPG MGLKGDLCER HGEKLKMFCK EDVLIMCEAC
SQSPEHEAHS VVPMEDVAWE YKWELHEALE HLKKEQEEAW KLEVGERKRT ATWKIQVETR
KQSIVWEFEK YQRLLEKKQP PHRQLGAEVA AALASLQREA AETMQKLELN HSELIQQSQV
LWRMIAELKE RSQRPVRWML QDIQEVLNRS KSWSLQQPEP ISLELKTDCR VLGLREILKT
YAADVRLDPD TAYSRLIVSE DRKRVHYGDT NQKLPDNPER FYRYNIVLGS QCISSGRHYW
EVEVGDRSEW GLGVCKQNVD RKEVVYLSPH YGFWVIRLRK GNEYRAGTDE YPILSLPVPP
RRVGIFVDYE AHDISFYNVT DCGSHIFTFP RYPFPGRLLP YFSPCYSIGT NNTAPLAICS
LDGED
