ID   APCL_HUMAN              Reviewed;        2303 AA.
AC   O95996; Q05BW4; Q9UBZ1; Q9UEM8; Q9UQJ8; Q9UQJ9; Q9Y632;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-OCT-2019, entry version 154.
DE   RecName: Full=Adenomatous polyposis coli protein 2;
DE   AltName: Full=Adenomatous polyposis coli protein-like;
DE            Short=APC-like;
GN   Name=APC2; Synonyms=APCL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   CTNNB1, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9823329;
RA   Nakagawa H., Murata Y., Koyama K., Fujiyama A., Miyoshi Y., Monden M.,
RA   Akiyama T., Nakamura Y.;
RT   "Identification of a brain-specific APC homologue, APCL, and its
RT   interaction with beta-catenin.";
RL   Cancer Res. 58:5176-5181(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=10551328; DOI=10.1111/j.1349-7006.1999.tb00845.x;
RA   Nakagawa H., Koyama K., Monden M., Nakamura Y.;
RT   "Analysis of APCL, a brain-specific adenomatous polyposis coli
RT   homologue, for mutations and expression in brain tumors.";
RL   Jpn. J. Cancer Res. 90:982-986(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-1521 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [GENOMIC DNA] OF 34-86 AND 476-555 (ISOFORM 2).
RA   Carr I.M., Markham A.F., Colleta P.L., Wai L., Askham J., Morrison E.,
RA   Meredith D.M.;
RT   "APC2 alternatively spliced cDNA sequence.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-731 (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP   [GENOMIC DNA] OF 618-2303 (ISOFORM 3), FUNCTION, INTERACTION WITH
RP   AXIN2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Kidney;
RX   PubMed=10021369; DOI=10.1016/s0960-9822(99)80024-4;
RA   van Es J.H., Kirkpatrick C., van de Wetering M., Molenaar M.,
RA   Miles A., Kuipers J., Destree O., Peifer M., Clevers H.;
RT   "Identification of APC2, a homologue of the adenomatous polyposis coli
RT   tumour suppressor.";
RL   Curr. Biol. 9:105-108(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-702 (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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INTERACTION WITH TP53BP2, AND SUBCELLULAR LOCATION.
RX   PubMed=10646860;
RA   Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
RT   "APCL, a central nervous system-specific homologue of adenomatous
RT   polyposis coli tumor suppressor, binds to p53-binding protein 2 and
RT   translocates it to the perinucleus.";
RL   Cancer Res. 60:101-105(2000).
RN   [8]
RP   INTERACTION WITH MAPRE1 AND MAPRE3, AND SUBCELLULAR LOCATION.
RC   TISSUE=Fetal brain;
RX   PubMed=10644998; DOI=10.1038/sj.onc.1203308;
RA   Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
RT   "EB3, a novel member of the EB1 family preferentially expressed in the
RT   central nervous system, binds to a CNS-specific APC homologue.";
RL   Oncogene 19:210-216(2000).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11691822;
RA   Jarrett C.R., Blancato J., Cao T., Bressette D.S., Cepeda M.,
RA   Young P.E., King C.R., Byers S.W.;
RT   "Human APC2 localization and allelic imbalance.";
RL   Cancer Res. 61:7978-7984(2001).
RN   [10]
RP   INVOLVEMENT IN SOTOS3, FUNCTION, SUBCELLULAR LOCATION, AND REGION.
RX   PubMed=25753423; DOI=10.1016/j.celrep.2015.02.011;
RA   Almuriekhi M., Shintani T., Fahiminiya S., Fujikawa A., Kuboyama K.,
RA   Takeuchi Y., Nawaz Z., Nadaf J., Kamel H., Kitam A.K., Samiha Z.,
RA   Mahmoud L., Ben-Omran T., Majewski J., Noda M.;
RT   "Loss-of-function mutation in APC2 causes Sotos syndrome features.";
RL   Cell Rep. 10:1585-1598(2015).
RN   [11]
RP   VARIANTS [LARGE SCALE ANALYSIS] SER-562 AND SER-2003.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [12] {ECO:0000305}
RP   VARIANT ASN-1921.
RX   PubMed=29120066; DOI=10.1111/cge.13171;
RA   Mejecase C., Mohand-Said S., El Shamieh S., Antonio A., Condroyer C.,
RA   Blanchard S., Letexier M., Saraiva J.P., Sahel J.A., Audo I.,
RA   Zeitz C.;
RT   "A novel nonsense variant in REEP6 is involved in a sporadic rod-cone
RT   dystrophy case.";
RL   Clin. Genet. 93:707-711(2018).
CC   -!- FUNCTION: Stabilizes microtubules and may regulate actin fiber
CC       dynamics through the activation of Rho family GTPases
CC       (PubMed:25753423). May also function in Wnt signaling by promoting
CC       the rapid degradation of CTNNB1 (PubMed:10021369, PubMed:11691822,
CC       PubMed:9823329). {ECO:0000269|PubMed:10021369,
CC       ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423,
CC       ECO:0000269|PubMed:9823329}.
CC   -!- SUBUNIT: Interacts with PSRC1 (By similarity). Interacts with APC,
CC       CTNNB1, MAPRE1, MAPRE3, TP53BP2 and possibly with AXIN2.
CC       {ECO:0000250, ECO:0000269|PubMed:10021369,
CC       ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:10646860,
CC       ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:9823329}.
CC   -!- INTERACTION:
CC       Q15691:MAPRE1; NbExp=3; IntAct=EBI-1053045, EBI-1004115;
CC       Q9UPY8:MAPRE3; NbExp=7; IntAct=EBI-1053045, EBI-726739;
CC       Q13625:TP53BP2; NbExp=4; IntAct=EBI-1053045, EBI-77642;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822,
CC       ECO:0000269|PubMed:25753423}. Golgi apparatus
CC       {ECO:0000269|PubMed:11691822}. Cytoplasm
CC       {ECO:0000269|PubMed:11691822}. Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:10646860}. Note=Associated with actin
CC       filaments (PubMed:11691822, PubMed:25753423). Associated with
CC       microtubule network (PubMed:10644998, PubMed:11691822,
CC       PubMed:25753423). {ECO:0000269|PubMed:10644998,
CC       ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O95996-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95996-2; Sequence=VSP_030106;
CC       Name=3;
CC         IsoId=O95996-3; Sequence=VSP_030107;
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC       Specifically expressed in the CNS. {ECO:0000269|PubMed:10021369,
CC       ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:9823329}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal brain.
CC       {ECO:0000269|PubMed:10021369}.
CC   -!- DISEASE: Sotos syndrome 3 (SOTOS3) [MIM:617169]: A form of Sotos
CC       syndrome, a childhood overgrowth syndrome characterized by
CC       prenatal and postnatal overgrowth, developmental delay, mental
CC       retardation, advanced bone age, and abnormal craniofacial
CC       morphology. SOTOS3 patients do not have advanced bone age,
CC       hypotonia, seizures, or autism. SOTOS3 transmission pattern is
CC       consistent with autosomal recessive inheritance.
CC       {ECO:0000269|PubMed:25753423}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD28183.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAF01784.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC       Sequence=CAA10317.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAB61207.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR   EMBL; AB012162; BAA34611.1; -; mRNA.
DR   EMBL; AB022529; BAA75469.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69498.1; -; Genomic_DNA.
DR   EMBL; AF110334; AAD28183.1; ALT_FRAME; mRNA.
DR   EMBL; AF110335; AAD29273.1; -; Genomic_DNA.
DR   EMBL; AF110337; AAD29274.1; -; Genomic_DNA.
DR   EMBL; AF110336; AAD29274.1; JOINED; Genomic_DNA.
DR   EMBL; AF128222; AAF01784.1; ALT_SEQ; mRNA.
DR   EMBL; AJ012652; CAB61207.1; ALT_SEQ; mRNA.
DR   EMBL; AJ131187; CAA10317.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC032573; AAH32573.1; -; mRNA.
DR   CCDS; CCDS12068.1; -. [O95996-1]
DR   RefSeq; NP_005874.1; NM_005883.2. [O95996-1]
DR   RefSeq; XP_006722672.1; XM_006722609.3. [O95996-1]
DR   SMR; O95996; -.
DR   BioGrid; 115585; 7.
DR   ComplexPortal; CPX-440; Beta-catenin destruction core complex, variant 4.
DR   ComplexPortal; CPX-442; Beta-catenin destruction core complex, variant 6.
DR   ComplexPortal; CPX-443; Beta-catenin destruction core complex, variant 8.
DR   ComplexPortal; CPX-99; Beta-catenin destruction core complex, variant 2.
DR   ELM; O95996; -.
DR   IntAct; O95996; 6.
DR   MINT; O95996; -.
DR   STRING; 9606.ENSP00000442954; -.
DR   CarbonylDB; O95996; -.
DR   iPTMnet; O95996; -.
DR   PhosphoSitePlus; O95996; -.
DR   BioMuta; APC2; -.
DR   jPOST; O95996; -.
DR   MassIVE; O95996; -.
DR   PaxDb; O95996; -.
DR   PeptideAtlas; O95996; -.
DR   PRIDE; O95996; -.
DR   ProteomicsDB; 51171; -. [O95996-1]
DR   ProteomicsDB; 51172; -. [O95996-2]
DR   ProteomicsDB; 51173; -. [O95996-3]
DR   Ensembl; ENST00000233607; ENSP00000233607; ENSG00000115266. [O95996-1]
DR   Ensembl; ENST00000535453; ENSP00000442954; ENSG00000115266. [O95996-1]
DR   GeneID; 10297; -.
DR   KEGG; hsa:10297; -.
DR   UCSC; uc002lsr.1; human. [O95996-1]
DR   CTD; 10297; -.
DR   DisGeNET; 10297; -.
DR   GeneCards; APC2; -.
DR   HGNC; HGNC:24036; APC2.
DR   HPA; HPA078002; -.
DR   MalaCards; APC2; -.
DR   MIM; 612034; gene.
DR   MIM; 617169; phenotype.
DR   neXtProt; NX_O95996; -.
DR   OpenTargets; ENSG00000115266; -.
DR   Orphanet; 821; Sotos syndrome.
DR   PharmGKB; PA134906843; -.
DR   eggNOG; KOG2122; Eukaryota.
DR   eggNOG; ENOG410XR2V; LUCA.
DR   GeneTree; ENSGT00530000063749; -.
DR   InParanoid; O95996; -.
DR   KO; K02085; -.
DR   OMA; AMPSKFR; -.
DR   OrthoDB; 31524at2759; -.
DR   PhylomeDB; O95996; -.
DR   TreeFam; TF106496; -.
DR   SignaLink; O95996; -.
DR   SIGNOR; O95996; -.
DR   ChiTaRS; APC2; human.
DR   GenomeRNAi; 10297; -.
DR   Pharos; O95996; -.
DR   PRO; PR:O95996; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000115266; Expressed in 173 organ(s), highest expression level in paraflocculus.
DR   ExpressionAtlas; O95996; baseline and differential.
DR   Genevisible; O95996; HS.
DR   GO; GO:0005884; C:actin filament; IDA:BHF-UCL.
DR   GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0031258; C:lamellipodium membrane; IDA:BHF-UCL.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
DR   GO; GO:0030496; C:midbody; IDA:HPA.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR   GO; GO:0045295; F:gamma-catenin binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
DR   GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR   GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
DR   GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR026837; APC2.
DR   InterPro; IPR009234; APC_basic_dom.
DR   InterPro; IPR026831; APC_dom.
DR   InterPro; IPR026818; Apc_fam.
DR   InterPro; IPR032038; APC_N.
DR   InterPro; IPR036149; APC_N_sf.
DR   InterPro; IPR041257; APC_rep.
DR   InterPro; IPR009223; APC_rpt.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR009224; SAMP.
DR   PANTHER; PTHR12607; PTHR12607; 1.
DR   PANTHER; PTHR12607:SF3; PTHR12607:SF3; 1.
DR   Pfam; PF05956; APC_basic; 1.
DR   Pfam; PF16689; APC_N_CC; 1.
DR   Pfam; PF05923; APC_r; 4.
DR   Pfam; PF18797; APC_rep; 1.
DR   Pfam; PF00514; Arm; 1.
DR   Pfam; PF05924; SAMP; 2.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF58050; SSF58050; 1.
DR   SUPFAM; SSF82931; SSF82931; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Golgi apparatus; Microtubule; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Wnt signaling pathway.
FT   CHAIN         1   2303       Adenomatous polyposis coli protein 2.
FT                                /FTId=PRO_0000313686.
FT   REPEAT      302    341       ARM 1.
FT   REPEAT      479    518       ARM 2.
FT   REPEAT      522    562       ARM 3.
FT   REPEAT      566    609       ARM 4.
FT   REPEAT      615    654       ARM 5.
FT   REPEAT      657    696       ARM 6.
FT   REPEAT     1058   1077       1.
FT   REPEAT     1150   1169       2.
FT   REPEAT     1263   1282       3.
FT   REPEAT     1391   1410       4.
FT   REPEAT     1568   1587       5.
FT   REGION     1058   1587       5 X 20 AA approximate repeat of F-X-V-E-
FT                                X-T-P-X-C-F-S-R-X-S-S-L-S-S-L-S.
FT   REGION     1058   1587       Interaction with CTNNB1.
FT                                {ECO:0000269|PubMed:9823329}.
FT   REGION     1821   1900       Required for localization to microtubules
FT                                and function in microtubule
FT                                stabilization.
FT                                {ECO:0000269|PubMed:25753423}.
FT   REGION     2067   2144       Interaction with MAPRE1 and MAPRE3.
FT                                {ECO:0000269|PubMed:10644998}.
FT   COILED        8     59       {ECO:0000255}.
FT   COILED      840    864       {ECO:0000255}.
FT   COMPBIAS   1145   1196       Ser-rich.
FT   COMPBIAS   1518   1622       Pro-rich.
FT   COMPBIAS   1765   1953       Pro-rich.
FT   MOD_RES    1585   1585       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z1K7}.
FT   MOD_RES    1587   1587       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z1K7}.
FT   VAR_SEQ     168    441       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_030106.
FT   VAR_SEQ     175    175       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:10021369}.
FT                                /FTId=VSP_030107.
FT   VARIANT     562    562       A -> S (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_037703.
FT   VARIANT    1921   1921       H -> N. {ECO:0000269|PubMed:29120066}.
FT                                /FTId=VAR_081224.
FT   VARIANT    2003   2003       G -> S (in a breast cancer sample;
FT                                somatic mutation; dbSNP:rs1288757495).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_037704.
FT   VARIANT    2241   2241       S -> A (in dbSNP:rs265277).
FT                                /FTId=VAR_037705.
FT   CONFLICT    463    463       Missing (in Ref. 4; AAD28183).
FT                                {ECO:0000305}.
FT   CONFLICT    526    527       KV -> NL (in Ref. 4; AAD28183/AAD29274).
FT                                {ECO:0000305}.
FT   CONFLICT    566    566       E -> A (in Ref. 5; AAF01784/CAB61207).
FT                                {ECO:0000305}.
FT   CONFLICT    816    816       L -> Q (in Ref. 4; AAD28183).
FT                                {ECO:0000305}.
FT   CONFLICT    971    971       L -> P (in Ref. 4; AAD28183).
FT                                {ECO:0000305}.
FT   CONFLICT   1106   1106       S -> I (in Ref. 4; AAD28183).
FT                                {ECO:0000305}.
FT   CONFLICT   1140   1140       E -> G (in Ref. 5; CAA10317).
FT                                {ECO:0000305}.
FT   CONFLICT   1188   1188       Q -> H (in Ref. 4; AAD28183).
FT                                {ECO:0000305}.
FT   CONFLICT   1361   1361       A -> G (in Ref. 4; AAD28183).
FT                                {ECO:0000305}.
FT   CONFLICT   1456   1456       R -> P (in Ref. 4; AAD28183).
FT                                {ECO:0000305}.
FT   CONFLICT   1515   1515       D -> V (in Ref. 4; AAD28183).
FT                                {ECO:0000305}.
FT   CONFLICT   2219   2219       A -> V (in Ref. 5; CAA10317).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2303 AA;  243949 MW;  7BF940183ACD643D CRC64;
     MASSVAPYEQ LVRQVEALKA ENSHLRQELR DNSSHLSKLE TETSGMKEVL KHLQGKLEQE
     ARVLVSSGQT EVLEQLKALQ MDITSLYNLK FQPPTLGPEP AARTPEGSPV HGSGPSKDSF
     GELSRATIRL LEELDRERCF LLNEIEKEEK EKLWYYSQLQ GLSKRLDELP HVETQFSMQM
     DLIRQQLEFE AQHIRSLMEE RFGTSDEMVQ RAQIRASRLE QIDKELLEAQ DRVQQTEPQA
     LLAVKSVPVD EDPETEVPTH PEDGTPQPGN SKVEVVFWLL SMLATRDQED TARTLLAMSS
     SPESCVAMRR SGCLPLLLQI LHGTEAAAGG RAGAPGAPGA KDARMRANAA LHNIVFSQPD
     QGLARKEMRV LHVLEQIRAY CETCWDWLQA RDGGPEGGGA GSAPIPIEPQ ICQATCAVMK
     LSFDEEYRRA MNELGGLQAV AELLQVDYEM HKMTRDPLNL ALRRYAGMTL TNLTFGDVAN
     KATLCARRGC MEAIVAQLAS DSEELHQVVS SILRNLSWRA DINSKKVLRE AGSVTALVQC
     VLRATKESTL KSVLSALWNL SAHSTENKAA ICQVDGALGF LVSTLTYKCQ SNSLAIIESG
     GGILRNVSSL VATREDYRQV LRDHNCLQTL LQHLTSHSLT IVSNACGTLW NLSARSARDQ
     ELLWDLGAVG MLRNLVHSKH KMIAMGSAAA LRNLLAHRPA KHQAAATAVS PGSCVPSLYV
     RKQRALEAEL DARHLAQALE HLEKQGPPAA EAATKKPLPP LRHLDGLAQD YASDSGCFDD
     DDAPSSLAAA AATGEPASPA ALSLFLGSPF LQGQALARTP PTRRGGKEAE KDTSGEAAVA
     AKAKAKLALA VARIDQLVED ISALHTSSDD SFSLSSGDPG QEAPREGRAQ SCSPCRGPEG
     GRREAGSRAH PLLRLKAAHA SLSNDSLNSG SASDGYCPRE HMLPCPLAAL ASRREDPRCG
     QPRPSRLDLD LPGCQAEPPA REATSADARV RTIKLSPTYQ HVPLLEGASR AGAEPLAGPG
     ISPGARKQAW LPADHLSKVP EKLAAAPLSV ASKALQKLAA QEGPLSLSRC SSLSSLSSAG
     RPGPSEGGDL DDSDSSLEGL EEAGPSEAEL DSTWRAPGAT SLPVAIPAPR RNRGRGLGVE
     DATPSSSSEN YVQETPLVLS RCSSVSSLGS FESPSIASSI PSEPCSGQGS GTISPSELPD
     SPGQTMPPSR SKTPPLAPAP QGPPEATQFS LQWESYVKRF LDIADCRERC RLPSELDAGS
     VRFTVEKPDE NFSCASSLSA LALHEHYVQQ DVELRLLPSA CPERGGGAGG AGLHFAGHRR
     REEGPAPTGS RPRGAADQEL ELLRECLGAA VPARLRKVAS ALVPGRRALP VPVYMLVPAP
     APAQEDDSCT DSAEGTPVNF SSAASLSDET LQGPPRDQPG GPAGRQRPTG RPTSARQAMG
     HRHKAGGAGR SAEQSRGAGK NRAGLELPLG RPPSAPADKD GSKPGRTRGD GALQSLCLTT
     PTEEAVYCFY GNDSDEEPPA AAPTPTHRRT SAIPRAFTRE RPQGRKEAPA PSKAAPAAPP
     PARTQPSLIA DETPPCYSLS SSASSLSEPE PSEPPAVHPR GREPAVTKDP GPGGGRDSSP
     SPRAAEELLQ RCISSALPRR RPPVSGLRRR KPRATRLDER PAEGSRERGE EAAGSDRASD
     LDSVEWRAIQ EGANSIVTWL HQAAAATREA SSESDSILSF VSGLSVGSTL QPPKHRKGRQ
     AEGEMGSARR PEKRGAASVK TSGSPRSPAG PEKPRGTQKT TPGVPAVLRG RTVIYVPSPA
     PRAQPKGTPG PRATPRKVAP PCLAQPAAPA KVPSPGQQRS RSLHRPAKTS ELATLSQPPR
     SATPPARLAK TPSSSSSQTS PASQPLPRKR PPVTQAAGAL PGPGASPVPK TPARTLLAKQ
     HKTQRSPVRI PFMQRPARRG PPPLARAVPE PGPRGRAGTE AGPGARGGRL GLVRVASALS
     SGSESSDRSG FRRQLTFIKE SPGLRRRRSE LSSAESAASA PQGASPRRGR PALPAVFLCS
     SRCEELRAAP RQGPAPARQR PPAARPSPGE RPARRTTSES PSRLPVRAPA ARPETVKRYA
     SLPHISVARR PDGAVPAAPA SADAARRSSD GEPRPLPRVA APGTTWRRIR DEDVPHILRS
     TLPATALPLR GSTPEDAPAG PPPRKTSDAV VQTEEVAAPK TNSSTSPSLE TREPPGAPAG
     GQLSLLGSDV DGPSLAKAPI SAPFVHEGLG VAVGGFPASR HGSPSRSARV PPFNYVPSPM
     VVAATTDSAA EKAPATASAT LLE
//