ID   ABTB3_HUMAN             Reviewed;        1104 AA.
AC   A6QL63; A4FU41; B3KXG3; C9J019; C9JK80; E9PHS4; Q3ZTQ4; Q52M89; Q6ZV99;
AC   Q8N245;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 3.
DT   28-JAN-2026, entry version 137.
DE   RecName: Full=Ankyrin repeat- and BTB/POZ domain-containing protein 3;
DE   AltName: Full=BTB/POZ domain-containing protein 11;
GN   Name=ABTB3 {ECO:0000312|HGNC:HGNC:23844}; Synonyms=BTBD11;
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] (ISOFORMS 4 AND 5), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 338-1104 (ISOFORM 3).
RC   TISSUE=Hippocampus, and Tongue;
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 GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 550-1104 (ISOFORM 1).
RA   Xu J., Xie Y., Mao Y.;
RT   "Characterization of a novel gene containing ANK repeats and BTB domain.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cortical and hippocampal inhibitory interneuron-specific
CC       protein localized at glutamatergic (excitatory) synapses, where it
CC       supports cell type-specific synaptic function.
CC       {ECO:0000250|UniProtKB:Q6GQW0}.
CC   -!- SUBUNIT: Interacts with core postsynaptic proteins, including DLG4;
CC       interaction with DLG4 stabilizes DLG4 at glutamatergic synapses.
CC       {ECO:0000250|UniProtKB:Q6GQW0}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=A6QL63-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A6QL63-2; Sequence=VSP_032802;
CC       Name=3;
CC         IsoId=A6QL63-3; Sequence=VSP_032803;
CC       Name=4;
CC         IsoId=A6QL63-4; Sequence=VSP_032801;
CC       Name=5;
CC         IsoId=A6QL63-5; Sequence=VSP_045802, VSP_045803;
CC   -!- INDUCTION: By all-trans retinoic acid (ATRA).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI01562.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI01564.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI46825.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAR21078.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC85963.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAW97799.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK091276; BAC03626.1; -; mRNA.
DR   EMBL; AK124835; BAC85963.1; ALT_INIT; mRNA.
DR   EMBL; AK127295; BAG54475.1; -; mRNA.
DR   EMBL; AC007540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC007649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC009774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW97799.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471054; EAW97800.1; -; Genomic_DNA.
DR   EMBL; BC093627; AAH93627.1; -; mRNA.
DR   EMBL; BC093629; AAH93629.1; -; mRNA.
DR   EMBL; BC101561; AAI01562.1; ALT_INIT; mRNA.
DR   EMBL; BC101563; AAI01564.1; ALT_INIT; mRNA.
DR   EMBL; BC146824; AAI46825.1; ALT_SEQ; mRNA.
DR   EMBL; AY373588; AAR21078.1; ALT_INIT; mRNA.
DR   CCDS; CCDS31893.1; -. [A6QL63-1]
DR   CCDS; CCDS41827.1; -. [A6QL63-5]
DR   CCDS; CCDS86332.1; -. [A6QL63-2]
DR   RefSeq; NP_001017523.1; NM_001017523.2. [A6QL63-5]
DR   RefSeq; NP_001018082.1; NM_001018072.2. [A6QL63-1]
DR   RefSeq; NP_001334872.1; NM_001347943.2. [A6QL63-2]
DR   AlphaFoldDB; A6QL63; -.
DR   SMR; A6QL63; -.
DR   BioGRID; 125738; 9.
DR   FunCoup; A6QL63; 171.
DR   IntAct; A6QL63; 6.
DR   STRING; 9606.ENSP00000280758; -.
DR   GlyGen; A6QL63; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; A6QL63; -.
DR   PhosphoSitePlus; A6QL63; -.
DR   BioMuta; BTBD11; -.
DR   jPOST; A6QL63; -.
DR   MassIVE; A6QL63; -.
DR   PaxDb; 9606-ENSP00000280758; -.
DR   PeptideAtlas; A6QL63; -.
DR   ProteomicsDB; 1742; -. [A6QL63-1]
DR   ProteomicsDB; 1743; -. [A6QL63-2]
DR   ProteomicsDB; 1744; -. [A6QL63-3]
DR   ProteomicsDB; 1745; -. [A6QL63-4]
DR   ProteomicsDB; 20594; -.
DR   Pumba; A6QL63; -.
DR   Antibodypedia; 76946; 9 antibodies from 8 providers.
DR   DNASU; 121551; -.
DR   Ensembl; ENST00000280758.10; ENSP00000280758.5; ENSG00000151136.15. [A6QL63-1]
DR   Ensembl; ENST00000357167.8; ENSP00000349690.4; ENSG00000151136.15. [A6QL63-5]
DR   Ensembl; ENST00000420571.6; ENSP00000413889.2; ENSG00000151136.15. [A6QL63-2]
DR   Ensembl; ENST00000490090.6; ENSP00000447319.1; ENSG00000151136.15. [A6QL63-3]
DR   Ensembl; ENST00000494235.2; ENSP00000448322.1; ENSG00000151136.15. [A6QL63-4]
DR   GeneID; 121551; -.
DR   KEGG; hsa:121551; -.
DR   MANE-Select; ENST00000280758.10; ENSP00000280758.5; NM_001018072.2; NP_001018082.1.
DR   UCSC; uc001tmj.4; human. [A6QL63-1]
DR   AGR; HGNC:23844; -.
DR   ClinPGx; PA134975180; -.
DR   CTD; 121551; -.
DR   DisGeNET; 121551; -.
DR   GeneCards; ABTB3; -.
DR   HGNC; HGNC:23844; ABTB3.
DR   HPA; ENSG00000151136; Tissue enhanced (esophagus, parathyroid gland).
DR   MIM; 621028; gene.
DR   OpenTargets; ENSG00000151136; -.
DR   VEuPathDB; HostDB:ENSG00000151136; -.
DR   eggNOG; ENOG502QSQY; Eukaryota.
DR   GeneTree; ENSGT00940000156419; -.
DR   HOGENOM; CLU_001918_0_0_1; -.
DR   InParanoid; A6QL63; -.
DR   OMA; NLHREPQ; -.
DR   OrthoDB; 2316821at2759; -.
DR   PAN-GO; A6QL63; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; A6QL63; -.
DR   PathwayCommons; A6QL63; -.
DR   SignaLink; A6QL63; -.
DR   Agora; ENSG00000151136; -.
DR   BioGRID-ORCS; 121551; 13 hits in 1187 CRISPR screens.
DR   ChiTaRS; BTBD11; human.
DR   GenomeRNAi; 121551; -.
DR   Pharos; A6QL63; Tdark.
DR   PRO; PR:A6QL63; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; A6QL63; protein.
DR   Bgee; ENSG00000151136; Expressed in lower esophagus mucosa and 147 other cell types or tissues.
DR   ExpressionAtlas; A6QL63; baseline and differential.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR   CDD; cd18527; BACK_BTBD11; 1.
DR   CDD; cd18351; BTB_POZ_BTBD11; 1.
DR   CDD; cd22913; HFD_ABTB2-like; 1.
DR   FunFam; 1.25.40.20:FF:000045; Ankyrin repeat and BTB/POZ domain-containing protein 2; 1.
DR   FunFam; 3.30.710.10:FF:000030; Ankyrin repeat and BTB/POZ domain-containing protein BTBD11; 1.
DR   FunFam; 1.10.20.10:FF:000060; BTB domain containing 11; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1.
DR   InterPro; IPR059008; ABTB2/3_histone.
DR   InterPro; IPR052089; Ankyrin-BTB/POZ_domain.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR047824; BTBD11_BACK.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR46071; ANKYRIN REPEAT AND BTB/POZ DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR46071:SF1; ANKYRIN REPEAT AND BTB_POZ DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF26281; Histone_ABTB; 1.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47113; Histone-fold; 2.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Membrane; Proteomics identification;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1104
FT                   /note="Ankyrin repeat- and BTB/POZ domain-containing
FT                   protein 3"
FT                   /id="PRO_0000328827"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          603..632
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          649..678
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          687..716
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          730..759
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          825..854
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          923..989
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REGION          260..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..276
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..921
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_032801"
FT   VAR_SEQ         1..33
FT                   /note="MARRGKKPVVRTLEDLTLDSGYGGAADSVRSSN -> MRKLRPKDSREPAPG
FT                   SPVRSGCLQRLSHYSGIQ (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045802"
FT   VAR_SEQ         34..496
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045803"
FT   VAR_SEQ         699..817
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032802"
FT   VAR_SEQ         998..1104
FT                   /note="LLSAAKFFQLEALQRHCEIICAKSINTDNCVDIYNHAKFLGVTELSAYCEGY
FT                   FLKNMMVLIENEAFKQLLYDKNGEGTGQDVLQDLQRTLAIRIQSIHLSSSKGSVV ->
FT                   VRDPLWCWLS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_032803"
FT   VARIANT         448
FT                   /note="G -> S (in dbSNP:rs1558781)"
FT                   /id="VAR_055560"
FT   VARIANT         1002
FT                   /note="A -> D (in dbSNP:rs11610050)"
FT                   /id="VAR_042534"
FT   VARIANT         1076
FT                   /note="G -> S (in dbSNP:rs12303478)"
FT                   /id="VAR_042535"
FT   CONFLICT        224
FT                   /note="R -> H (in Ref. 4; AAI46825)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        361
FT                   /note="I -> V (in Ref. 1; BAC85963)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        653
FT                   /note="A -> V (in Ref. 1; BAG54475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1043
FT                   /note="S -> P (in Ref. 1; BAC03626)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1104 AA;  120884 MW;  118D5C668CB78A3E CRC64;
     MARRGKKPVV RTLEDLTLDS GYGGAADSVR SSNLSLCCSD SHPASPYGGS CWPPLADSMH
     SRHNSFDTVN TALVEDSEGL DCAGQHCSRL LPDLDEVPWT LQELEALLLR SRDPRAGPAV
     PGGLPKDALA KLSTLVSRAL VRIAKEAQRL SLRFAKCTKY EIQSAMEIVL SWGLAAHCTA
     AALAALSLYN MSSAGGDRLG RGKSARCGLT FSVGRVYRWM VDSRVALRIH EHAAIYLTAC
     MESLFRDIYS RVVASGVPRS CSGPGSGSGS GPGPSSGPGA APAADKEREA PGGGAASGGA
     CSAASSASGG SSCCAPPAAA AAAVPPAAAA NHHHHHHHAL HEAPKFTVET LEHTVNNDSE
     IWGLLQPYQH LICGKNASGV LCLPDSLNLH RDPQRSNKPG ELPMFSQSEL RTIEQSLLAT
     RVGSIAELSD LVSRAMHHLQ PLNAKHHGNG TPLHHKQGAL YWEPEALYTL CYFMHCPQME
     WENPNVEPSK VNLQVERPFL VLPPLMEWIR VAVAHAGHRR SFSMDSDDVR QAARLLLPGV
     DCEPRQLRAD DCFCASRKLD AVAIEAKFKQ DLGFRMLNCG RTDLVKQAVS LLGPDGINTM
     SEQGMTPLMY ACVRGDEAMV QMLLDAGADL NVEVVSTPHK YPSVHPETRH WTALTFAVLH
     GHIPVVQLLL DAGAKVEGSV EHGEENYSET PLQLAAAVGN FELVSLLLER GADPLIGTMY
     RNGISTTPQG DMNSFSQAAA HGHRNVFRKL LAQPEKEKSD ILSLEEILAE GTDLAETAPP
     PLCASRNSKA KLRALREAMY HSAEHGYVDV TIDIRSIGVP WTLHTWLESL RIAFQQHRRP
     LIQCLLKEFK TIQEEEYTEE LVTQGLPLMF EILKASKNEV ISQQLCVIFT HCYGPYPIPK
     LTEIKRKQTS RLDPHFLNNK EMSDVTFLVE GRPFYAHKVL LFTASPRFKA LLSSKPTNDG
     TCIEIGYVKY SIFQLVMQYL YYGGPESLLI KNNEIMELLS AAKFFQLEAL QRHCEIICAK
     SINTDNCVDI YNHAKFLGVT ELSAYCEGYF LKNMMVLIEN EAFKQLLYDK NGEGTGQDVL
     QDLQRTLAIR IQSIHLSSSK GSVV
//