ID   VPS8_HUMAN              Reviewed;        1428 AA.
AC   Q8N3P4; A8K8Q8; B9EIQ1; C9JB61; O94896; Q63HP2; Q9BVP9; Q9H9B0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Vacuolar protein sorting-associated protein 8 homolog;
GN   Name=VPS8; Synonyms=KIAA0804;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 608-1428 (ISOFORM 1).
RC   TISSUE=Teratocarcinoma, and Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 100-1428 (ISOFORM 1), AND VARIANTS VAL-83 AND
RP   TYR-1165.
RC   TISSUE=Amygdala, and Colon endothelium;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, 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 218-1428 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-32 AND SER-127, AND
RP   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   [10]
RP   FUNCTION OF THE CORVET COMPLEX, INTERACTION WITH TGFBRAP1, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=25266290; DOI=10.1111/tra.12232;
RA   Perini E.D., Schaefer R., Stoeter M., Kalaidzidis Y., Zerial M.;
RT   "Mammalian CORVET is required for fusion and conversion of distinct early
RT   endosome subpopulations.";
RL   Traffic 15:1366-1389(2014).
CC   -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking of the
CC       endocytic membrane transport pathway. Believed to act as a component of
CC       the putative CORVET endosomal tethering complexes which is proposed to
CC       be involved in the Rab5-to-Rab7 endosome conversion probably
CC       implicating MON1A/B, and via binding SNAREs and SNARE complexes to
CC       mediate tethering and docking events during SNARE-mediated membrane
CC       fusion. The CORVET complex is proposed to function as a Rab5 effector
CC       to mediate early endosome fusion probably in specific endosome
CC       subpopulations (PubMed:25266290). Functions predominantly in APPL1-
CC       containing endosomes (PubMed:25266290). {ECO:0000269|PubMed:25266290,
CC       ECO:0000305|PubMed:25266290}.
CC   -!- SUBUNIT: Interacts with RAB5C (By similarity). Interacts with TGFBRAP1
CC       (PubMed:25266290). Component of the putative class C core
CC       vacuole/endosome tethering (CORVET) complex; the core of which composed
CC       of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, is
CC       associated with VPS8 and TGFBRAP1 (PubMed:25266290).
CC       {ECO:0000250|UniProtKB:Q0P5W1, ECO:0000269|PubMed:25266290,
CC       ECO:0000305|PubMed:25266290}.
CC   -!- INTERACTION:
CC       Q8N3P4; Q8WUH2: TGFBRAP1; NbExp=2; IntAct=EBI-7261494, EBI-2954829;
CC   -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:25266290}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8N3P4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N3P4-2; Sequence=VSP_023249, VSP_023250;
CC       Name=3;
CC         IsoId=Q8N3P4-3; Sequence=VSP_023249;
CC   -!- SIMILARITY: Belongs to the VPS8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14322.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAH56195.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAH56195.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK022945; BAB14322.1; ALT_INIT; mRNA.
DR   EMBL; AK292423; BAF85112.1; -; mRNA.
DR   EMBL; AL833838; CAD38698.1; -; mRNA.
DR   EMBL; BX647915; CAH56195.1; ALT_FRAME; mRNA.
DR   EMBL; AC025573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001001; AAH01001.2; -; mRNA.
DR   EMBL; BC140768; AAI40769.1; -; mRNA.
DR   EMBL; AB018347; BAA34524.1; -; mRNA.
DR   CCDS; CCDS46971.1; -. [Q8N3P4-1]
DR   CCDS; CCDS46972.1; -. [Q8N3P4-3]
DR   RefSeq; NP_001009921.1; NM_001009921.2. [Q8N3P4-1]
DR   RefSeq; NP_056118.2; NM_015303.3. [Q8N3P4-3]
DR   RefSeq; XP_005247308.1; XM_005247251.3.
DR   AlphaFoldDB; Q8N3P4; -.
DR   SMR; Q8N3P4; -.
DR   BioGRID; 116937; 64.
DR   ComplexPortal; CPX-6213; CORVET tethering complex.
DR   CORUM; Q8N3P4; -.
DR   IntAct; Q8N3P4; 25.
DR   MINT; Q8N3P4; -.
DR   STRING; 9606.ENSP00000487164; -.
DR   TCDB; 8.A.225.1.1; the vacuolar protein sorting-associated protein (vps) family.
DR   GlyGen; Q8N3P4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8N3P4; -.
DR   MetOSite; Q8N3P4; -.
DR   PhosphoSitePlus; Q8N3P4; -.
DR   BioMuta; VPS8; -.
DR   DMDM; 296452997; -.
DR   EPD; Q8N3P4; -.
DR   jPOST; Q8N3P4; -.
DR   MassIVE; Q8N3P4; -.
DR   MaxQB; Q8N3P4; -.
DR   PaxDb; 9606-ENSP00000404704; -.
DR   PeptideAtlas; Q8N3P4; -.
DR   ProteomicsDB; 71820; -. [Q8N3P4-1]
DR   ProteomicsDB; 71821; -. [Q8N3P4-2]
DR   ProteomicsDB; 71822; -. [Q8N3P4-3]
DR   Pumba; Q8N3P4; -.
DR   Antibodypedia; 33827; 82 antibodies from 21 providers.
DR   DNASU; 23355; -.
DR   Ensembl; ENST00000436792.6; ENSP00000404704.2; ENSG00000156931.16. [Q8N3P4-3]
DR   Ensembl; ENST00000446204.6; ENSP00000405483.2; ENSG00000156931.16. [Q8N3P4-2]
DR   Ensembl; ENST00000625842.3; ENSP00000487164.1; ENSG00000156931.16. [Q8N3P4-1]
DR   GeneID; 23355; -.
DR   KEGG; hsa:23355; -.
DR   MANE-Select; ENST00000625842.3; ENSP00000487164.1; NM_001009921.3; NP_001009921.1.
DR   UCSC; uc003fpb.2; human. [Q8N3P4-1]
DR   AGR; HGNC:29122; -.
DR   CTD; 23355; -.
DR   DisGeNET; 23355; -.
DR   GeneCards; VPS8; -.
DR   HGNC; HGNC:29122; VPS8.
DR   HPA; ENSG00000156931; Low tissue specificity.
DR   MIM; 618366; gene.
DR   neXtProt; NX_Q8N3P4; -.
DR   OpenTargets; ENSG00000156931; -.
DR   PharmGKB; PA142671617; -.
DR   PharmGKB; PA142671888; -.
DR   VEuPathDB; HostDB:ENSG00000156931; -.
DR   eggNOG; KOG2079; Eukaryota.
DR   GeneTree; ENSGT00390000010672; -.
DR   HOGENOM; CLU_000917_1_2_1; -.
DR   InParanoid; Q8N3P4; -.
DR   OMA; WAHQDKH; -.
DR   OrthoDB; 120292at2759; -.
DR   PhylomeDB; Q8N3P4; -.
DR   TreeFam; TF314244; -.
DR   PathwayCommons; Q8N3P4; -.
DR   SignaLink; Q8N3P4; -.
DR   SIGNOR; Q8N3P4; -.
DR   BioGRID-ORCS; 23355; 42 hits in 1206 CRISPR screens.
DR   ChiTaRS; VPS8; human.
DR   GenomeRNAi; 23355; -.
DR   Pharos; Q8N3P4; Tbio.
DR   PRO; PR:Q8N3P4; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8N3P4; Protein.
DR   Bgee; ENSG00000156931; Expressed in adrenal tissue and 199 other cell types or tissues.
DR   ExpressionAtlas; Q8N3P4; baseline and differential.
DR   GO; GO:0033263; C:CORVET complex; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IMP:UniProtKB.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0035542; P:regulation of SNARE complex assembly; NAS:ComplexPortal.
DR   CDD; cd16687; RING-H2_Vps8; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR045111; Vps41/Vps8.
DR   InterPro; IPR025941; Vps8_central_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12616; VACUOLAR PROTEIN SORTING VPS41; 1.
DR   PANTHER; PTHR12616:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 8 HOMOLOG; 1.
DR   Pfam; PF12816; Vps8; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q8N3P4; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endosome; Metal-binding; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport; WD repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1428
FT                   /note="Vacuolar protein sorting-associated protein 8
FT                   homolog"
FT                   /id="PRO_0000278267"
FT   REPEAT          195..236
FT                   /note="WD"
FT   ZN_FING         1258..1310
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1330..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         179..180
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_023249"
FT   VAR_SEQ         578..667
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_023250"
FT   VARIANT         83
FT                   /note="I -> V (in dbSNP:rs9830734)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_030730"
FT   VARIANT         1165
FT                   /note="H -> Y (in dbSNP:rs11555405)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_030731"
FT   VARIANT         1364
FT                   /note="I -> T (in dbSNP:rs3821750)"
FT                   /id="VAR_030732"
FT   VARIANT         1372
FT                   /note="R -> H (in dbSNP:rs16859527)"
FT                   /id="VAR_030733"
FT   CONFLICT        433
FT                   /note="E -> G (in Ref. 2; CAH56195)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471
FT                   /note="K -> N (in Ref. 2; CAH56195)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        765
FT                   /note="A -> S (in Ref. 1; BAB14322)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        932
FT                   /note="Missing (in Ref. 2; CAH56195)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1042
FT                   /note="T -> A (in Ref. 1; BAB14322)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1043
FT                   /note="Q -> L (in Ref. 2; CAH56195)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1167
FT                   /note="E -> G (in Ref. 1; BAB14322)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1428 AA;  161754 MW;  97FB5E8D453BBCB6 CRC64;
     MENEPDHENV EQSLCAKTSE EELNKSFNLE ASLSKFSYID MDKELEFKND LIDDKEFDIP
     QVDTPPTLES ILNETDDEDE SFILEDPTLL NIDTIDSHSY DTSSVASSDS GDRTNLKRKK
     KLPDSFSLHG SVMRHSLLKG ISAQIVSAAD KVDAGLPTAI AVSSLIAVGT SHGLALIFGK
     DQNQALRLCL GSTSVGGQYG AISALSINND CSRLLCGFAK GQITMWDLAS GKLLRSITDA
     HPPGTAILHI KFTDDPTLAI CNDSGGSVFE LTFKRVMGVR TCESRCLFSG SKGEVCCIEP
     LHSKPELKDH PITQFSLLAM ASLTKILVIG LKPSLKVWMT FPYGRMDPSS VPLLAWHFVA
     VQNYVNPMLA FCRGDVVHFL LVKRDESGAI HVTKQKHLHL YYDLINFTWI NSRTVVLLDS
     VEKLHVIDRQ TQEELETVEI SEVQLVYNSS HFKSLATGGN VSQALALVGE KACYQSISSY
     GGQIFYLGTK SVYVMMLRSW RERVDHLLKQ DCLTEALALA WSFHEGKAKA VVGLSGDASK
     RKAIVADRMV EILFHYADRA LKKCPDQGKI QVMEQHFQDM VPVIVDYCLL LQRKDLLFSQ
     MYDKLSENSV AKGVFLECLE PYILSDKLVG ITPQVMKDLI VHFQDKKLME NVEALIVHMD
     ITSLDIQQVV LMCWENRLYD AMIYVYNRGM NEFISPMEKL FRVIAPPLNA GKTLTDEQVV
     MGNKLLVYIS CCLAGRAYPL GDIPEDLVPL VKNQVFEFLI RLHSAEASPE EEIYPYIRTL
     LHFDTREFLN VLALTFEDFK NDKQAVEYQQ RIVDILLKVM VENSDFTPSQ VGCLFTFLAR
     QLAKPDNTLF VNRTLFDQVL EFLCSPDDDS RHSERQQVLL ELLQAGGIVQ FEESRLIRMA
     EKAEFYQICE FMYEREHQYD KIIDCYLRDP LREEEVFNYI HNILSIPGHS AEEKQSVWQK
     AMDHIEELVS LKPCKAAELV ATHFSGHIET VIKKLQNQVL LFKFLRSLLD PREGIHVNQE
     LLQISPCITE QFIELLCQFN PTQVIETLQV LECYRLEETI QITQKYQLHE VTAYLLEKKG
     DIHGAFLIML ERLQSKLQEV THQGENTKED PSLKDVEDTM VETIALCQRN SHNLNQQQRE
     ALWFPLLEAM MAPQKLSSSA IPHLHSEALK SLTMQVLNSM AAFIALPSIL QRILQDPVYG
     KGKLGEIQGL ILGMLDTFNY EQTLLETTTS LLNQDLHWSL CNLRASVTRG LNPKQDYCSI
     CLQQYKRRQE MADEIIVFSC GHLYHSFCLQ NKECTVEFEG QTRWTCYKCS SSNKVGKLSE
     NSSEIKKGRI TPSQVKMSPS YHQSKGDPTA KKGTSEPVLD PQQIQAFDQL CRLYRGSSRL
     ALLTELSQNR SSESYRPFSG SQSAPAFNSI FQNENFQLQL IPPPVTED
//