ID   DJC11_HUMAN             Reviewed;         559 AA.
AC   Q9NVH1; Q4VWF5; Q5VZN0; Q6PK20; Q6PK70; Q8NDM2; Q96CL7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   28-JAN-2026, entry version 182.
DE   RecName: Full=DnaJ homolog subfamily C member 11;
GN   Name=DNAJC11;
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).
RA   Xu J., Xie Y., Mao Y.;
RT   "Identification of a novel human DNAJ domain-containing protein.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-267.
RC   TISSUE=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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP   SER-290.
RC   TISSUE=Brain, Lung, and 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-559 (ISOFORM 1).
RC   TISSUE=Mammary cancer;
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   SUBUNIT.
RX   PubMed=17624330; DOI=10.1016/j.febslet.2007.06.052;
RA   Xie J., Marusich M.F., Souda P., Whitelegge J., Capaldi R.A.;
RT   "The mitochondrial inner membrane protein mitofilin exists as a complex
RT   with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-
RT   containing protein 3 and 6 and DnaJC11.";
RL   FEBS Lett. 581:3545-3549(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX   PubMed=25111180; DOI=10.1371/journal.pone.0104237;
RA   Ioakeimidis F., Ott C., Kozjak-Pavlovic V., Violitzi F., Rinotas V.,
RA   Makrinou E., Eliopoulos E., Fasseas C., Kollias G., Douni E.;
RT   "A splicing mutation in the novel mitochondrial protein DNAJC11 causes
RT   motor neuron pathology associated with cristae disorganization, and
RT   lymphoid abnormalities in mice.";
RL   PLoS ONE 9:E104237-E104237(2014).
RN   [10]
RP   INTERACTION WITH THE MICOS COMPLEX, INTERACTION WITH SAM COMPLEX, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=25997101; DOI=10.7554/elife.06265;
RA   Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA   Gygi S.P., Van Vactor D., Harper J.W.;
RT   "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT   and cristae morphology.";
RL   Elife 4:0-0(2015).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: [Isoform 1]: Required for mitochondrial inner membrane
CC       organization. Seems to function through its association with the MICOS
CC       complex and the mitochondrial outer membrane sorting assembly machinery
CC       (SAM) complex. {ECO:0000269|PubMed:25111180, ECO:0000305}.
CC   -!- SUBUNIT: Associates with the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC       CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC       and QIL1/MIC13. This complex was also known under the names MINOS or
CC       MitOS complex. The MICOS complex associates with mitochondrial outer
CC       membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC       components of the mitochondrial outer membrane sorting assembly
CC       machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC       protein TMEM11 and with HSPA9 (PubMed:25997101). The MICOS and SAM
CC       complexes together with DNAJC11 are part of a large protein complex
CC       spanning both mitochondrial membranes termed the mitochondrial
CC       intermembrane space bridging (MIB) complex.
CC       {ECO:0000269|PubMed:17624330, ECO:0000269|PubMed:25997101,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9NVH1; Q9NVT9: ARMC1; NbExp=3; IntAct=EBI-1055336, EBI-3506974;
CC       Q9NVH1; P42858: HTT; NbExp=3; IntAct=EBI-1055336, EBI-466029;
CC       Q9NVH1; Q9BS40: LXN; NbExp=3; IntAct=EBI-1055336, EBI-1044504;
CC       Q9NVH1; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-1055336, EBI-11339910;
CC       Q9NVH1; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-1055336, EBI-2799833;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25997101}.
CC       Note=Isoforms show differential submitochondrial localization. A 57 kDa
CC       form (potentially isoform 3) shows either mitochondrial matrix or
CC       innermembrane (IM) localization, possibly anchored to the IM facing the
CC       matrix. A 35 kDa form behaved either as an inner membrane space (IMS)
CC       or an IM protein exposed to the IMS. {ECO:0000269|PubMed:25111180}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:25111180}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:25111180}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist.
CC         {ECO:0000305|PubMed:25111180};
CC       Name=1;
CC         IsoId=Q9NVH1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NVH1-2; Sequence=VSP_019933;
CC       Name=3;
CC         IsoId=Q9NVH1-3; Sequence=VSP_019932;
CC   -!- SIMILARITY: Belongs to the DNAJC11 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH08772.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY336749; AAR02411.1; -; mRNA.
DR   EMBL; AK001599; BAA91780.1; -; mRNA.
DR   EMBL; AL031447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL159177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006086; AAH06086.1; -; mRNA.
DR   EMBL; BC008772; AAH08772.1; ALT_INIT; mRNA.
DR   EMBL; BC014145; AAH14145.1; -; mRNA.
DR   EMBL; AL833841; CAD38701.1; -; mRNA.
DR   CCDS; CCDS87.1; -. [Q9NVH1-1]
DR   RefSeq; NP_060668.2; NM_018198.4. [Q9NVH1-1]
DR   AlphaFoldDB; Q9NVH1; -.
DR   SMR; Q9NVH1; -.
DR   BioGRID; 120854; 261.
DR   CORUM; Q9NVH1; -.
DR   FunCoup; Q9NVH1; 3551.
DR   IntAct; Q9NVH1; 148.
DR   MINT; Q9NVH1; -.
DR   STRING; 9606.ENSP00000366800; -.
DR   GlyGen; Q9NVH1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NVH1; -.
DR   PhosphoSitePlus; Q9NVH1; -.
DR   SwissPalm; Q9NVH1; -.
DR   BioMuta; DNAJC11; -.
DR   DMDM; 110808199; -.
DR   jPOST; Q9NVH1; -.
DR   MassIVE; Q9NVH1; -.
DR   PaxDb; 9606-ENSP00000366800; -.
DR   PeptideAtlas; Q9NVH1; -.
DR   ProteomicsDB; 82796; -. [Q9NVH1-1]
DR   ProteomicsDB; 82797; -. [Q9NVH1-2]
DR   ProteomicsDB; 82798; -. [Q9NVH1-3]
DR   Pumba; Q9NVH1; -.
DR   Antibodypedia; 27462; 110 antibodies from 24 providers.
DR   DNASU; 55735; -.
DR   Ensembl; ENST00000294401.11; ENSP00000294401.7; ENSG00000007923.18. [Q9NVH1-3]
DR   Ensembl; ENST00000377577.10; ENSP00000366800.5; ENSG00000007923.18. [Q9NVH1-1]
DR   GeneID; 55735; -.
DR   KEGG; hsa:55735; -.
DR   MANE-Select; ENST00000377577.10; ENSP00000366800.5; NM_018198.4; NP_060668.2.
DR   UCSC; uc001aof.3; human. [Q9NVH1-1]
DR   AGR; HGNC:25570; -.
DR   ClinPGx; PA134893823; -.
DR   CTD; 55735; -.
DR   DisGeNET; 55735; -.
DR   GeneCards; DNAJC11; -.
DR   HGNC; HGNC:25570; DNAJC11.
DR   HPA; ENSG00000007923; Low tissue specificity.
DR   MIM; 614827; gene.
DR   OpenTargets; ENSG00000007923; -.
DR   VEuPathDB; HostDB:ENSG00000007923; -.
DR   eggNOG; KOG0718; Eukaryota.
DR   GeneTree; ENSGT00860000133842; -.
DR   HOGENOM; CLU_019611_2_0_1; -.
DR   InParanoid; Q9NVH1; -.
DR   OMA; QLDKHTM; -.
DR   OrthoDB; 18010at2759; -.
DR   PAN-GO; Q9NVH1; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; Q9NVH1; -.
DR   PathwayCommons; Q9NVH1; -.
DR   Reactome; R-HSA-8949613; Cristae formation.
DR   SignaLink; Q9NVH1; -.
DR   SIGNOR; Q9NVH1; -.
DR   Agora; ENSG00000007923; -.
DR   BioGRID-ORCS; 55735; 504 hits in 1178 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; DNAJC11; human.
DR   GeneWiki; DNAJC11; -.
DR   GenomeRNAi; 55735; -.
DR   Pharos; Q9NVH1; Tbio.
DR   PRO; PR:Q9NVH1; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9NVH1; protein.
DR   Bgee; ENSG00000007923; Expressed in metanephros cortex and 198 other cell types or tissues.
DR   ExpressionAtlas; Q9NVH1; baseline and differential.
DR   GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IMP:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
DR   GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
DR   GO; GO:0007007; P:inner mitochondrial membrane organization; IC:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   FunFam; 1.10.287.110:FF:000027; DnaJ (Hsp40) homolog, subfamily C, member 11; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR024586; DnaJ-like_C11_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR055225; DNAJC11-like_beta-barrel.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR052243; Mito_inner_membrane_organizer.
DR   PANTHER; PTHR44157; DNAJ HOMOLOG SUBFAMILY C MEMBER 11; 1.
DR   PANTHER; PTHR44157:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 11; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF11875; DnaJ-like_C11_C; 1.
DR   Pfam; PF22774; DNAJC11_beta-barrel; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chaperone; Coiled coil; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW   Proteomics identification; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..559
FT                   /note="DnaJ homolog subfamily C member 11"
FT                   /id="PRO_0000247157"
FT   DOMAIN          14..82
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   COILED          417..457
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5U458"
FT   VAR_SEQ         367..418
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019932"
FT   VAR_SEQ         465..502
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_019933"
FT   VARIANT         267
FT                   /note="V -> M (in dbSNP:rs12137794)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_027078"
FT   VARIANT         290
FT                   /note="T -> A (in dbSNP:rs200454)"
FT                   /id="VAR_027079"
FT   VARIANT         290
FT                   /note="T -> S (in dbSNP:rs200454)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_055703"
FT   CONFLICT        309
FT                   /note="S -> I (in Ref. 1; BAA91780)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   559 AA;  63278 MW;  B16D49B296362800 CRC64;
     MATALSEEEL DNEDYYSLLN VRREASSEEL KAAYRRLCML YHPDKHRDPE LKSQAERLFN
     LVHQAYEVLS DPQTRAIYDI YGKRGLEMEG WEVVERRRTP AEIREEFERL QREREERRLQ
     QRTNPKGTIS VGVDATDLFD RYDEEYEDVS GSSFPQIEIN KMHISQSIEA PLTATDTAIL
     SGSLSTQNGN GGGSINFALR RVTSAKGWGE LEFGAGDLQG PLFGLKLFRN LTPRCFVTTN
     CALQFSSRGI RPGLTTVLAR NLDKNTVGYL QWRWGIQSAM NTSIVRDTKT SHFTVALQLG
     IPHSFALISY QHKFQDDDQT RVKGSLKAGF FGTVVEYGAE RKISRHSVLG AAVSVGVPQG
     VSLKVKLNRA SQTYFFPIHL TDQLLPSAMF YATVGPLVVY FAMHRLIIKP YLRAQKEKEL
     EKQRESAATD VLQKKQEAES AVRLMQESVR RIIEAEESRM GLIIVNAWYG KFVNDKSRKS
     EKVKVIDVTV PLQCLVKDSK LILTEASKAG LPGFYDPCVG EEKNLKVLYQ FRGVLHQVMV
     LDSEALRIPK QSHRIDTDG
//