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Keratin, type II cytoskeletal 6A (Cytokeratin-6A) (CK-6A) (Cytokeratin-6D) (CK-6D) (Keratin-6A) (K6A) (Type-II keratin Kb6) (allergen Hom s 5)

 K2C6A_HUMAN             Reviewed;         564 AA.
P02538; A4QPC1; P48667; Q08AR4; Q6NT67; Q96CL4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 181.
RecName: Full=Keratin, type II cytoskeletal 6A;
AltName: Full=Cytokeratin-6A;
Short=CK-6A;
AltName: Full=Cytokeratin-6D;
Short=CK-6D;
AltName: Full=Keratin-6A;
Short=K6A;
AltName: Full=Type-II keratin Kb6;
AltName: Allergen=Hom s 5;
Name=KRT6A; Synonyms=K6A, KRT6D;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Skin;
PubMed=7543104; DOI=10.1074/jbc.270.31.18581;
Takahashi K., Paladini R.D., Coulombe P.A.;
"Cloning and characterization of multiple human genes and cDNAs
encoding highly related type II keratin 6 isoforms.";
J. Biol. Chem. 270:18581-18592(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-21.
TISSUE=Brain, Ovary, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-9; 31-40; 43-86; 169-204; 208-232; 241-347;
350-369; 379-386; 425-436; 447-475 AND 534-550, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N., Lilla S., Lange E.,
Sumpton D.P.;
Submitted (MAR-2008) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 208-564.
PubMed=6191871; DOI=10.1016/0092-8674(83)90034-X;
Hanukoglu I., Fuchs E.;
"The cDNA sequence of a type II cytoskeletal keratin reveals constant
and variable structural domains among keratins.";
Cell 33:915-924(1983).
[6]
INTERACTION WITH TCHP.
PubMed=15731013; DOI=10.1242/jcs.01667;
Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T.,
Usukura J., Inagaki M.;
"Identification of trichoplein, a novel keratin filament-binding
protein.";
J. Cell Sci. 118:1081-1090(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
INVOLVEMENT IN PC3.
PubMed=22668561; DOI=10.1684/ejd.2012.1773;
Du Z.F., Xu C.M., Zhao Y., Liu W.T., Chen X.L., Chen C.Y., Fang H.,
Ke H.P., Zhang X.N.;
"Two novel de novo mutations of KRT6A and KRT16 genes in two Chinese
pachyonychia congenita pedigrees with fissured tongue or diffuse
plantar keratoderma.";
Eur. J. Dermatol. 22:476-480(2012).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
VARIANT PC3 ASN-171 DEL.
PubMed=7545493; DOI=10.1038/ng0795-363;
Bowden P.E., Haley J.L., Kansky A., Rothnagel J.A., Jones D.O.,
Turner R.J.;
"Mutation of a type II keratin gene (K6a) in pachyonychia congenita.";
Nat. Genet. 10:363-365(1995).
[11]
VARIANTS PC3 LYS-171 AND SER-174.
PubMed=10232400; DOI=10.1111/j.1600-0625.1999.tb00356.x;
Smith F.J., McKenna K.E., Irvine A.D., Bingham E.A., Coleman C.M.,
Uitto J., McLean W.H.;
"A mutation detection strategy for the human keratin 6A gene and novel
missense mutations in two cases of pachyonychia congenita type 1.";
Exp. Dermatol. 8:109-114(1999).
[12]
VARIANTS PC3 VAL-174; ARG-469 AND LYS-472.
PubMed=11886499; DOI=10.1046/j.0022-202x.2001.01565.x;
Terrinoni A., Smith F.J.D., Didona B., Canzona F., Paradisi M.,
Huber M., Hohl D., David A., Verloes A., Leigh I.M., Munro C.S.,
Melino G., McLean W.H.I.;
"Novel and recurrent mutations in the genes encoding keratins K6a, K16
and K17 in 13 cases of pachyonychia congenita.";
J. Invest. Dermatol. 117:1391-1396(2001).
[13]
VARIANT PC3 SER-462.
PubMed=15387942;
Kang X.J., Sun M., Yang W., Yu M., Ju Q., Lo W.H., Xia L.Q., Zhang X.;
"[A de nono I462S mutation in the KRT6A gene is associated with
pachyonychia congenita type I].";
Zhonghua Yi Xue Za Zhi 84:1344-1347(2004).
[14]
VARIANT PC3 PRO-464.
PubMed=15840119; DOI=10.1111/j.1365-2133.2005.06473.x;
Garcia-Rio I., Penas P.F., Garcia-Diez A., McLean W.H., Smith F.J.;
"A severe case of pachyonychia congenita type I due to a novel proline
mutation in keratin 6a.";
Br. J. Dermatol. 152:800-802(2005).
[15]
VARIANTS PC3 ASN-167; PHE-170; LYS-171; ASN-171 DEL; SER-171; SER-174;
PRO-176; ASN-462; PRO-468 AND PRO-469.
PubMed=16250206; DOI=10.1111/j.1087-0024.2005.10204.x;
Smith F.J., Liao H., Cassidy A.J., Stewart A., Hamill K.J., Wood P.,
Joval I., van Steensel M.A., Bjoerck E., Callif-Daley F., Pals G.,
Collins P., Leachman S.A., Munro C.S., McLean W.H.;
"The genetic basis of pachyonychia congenita.";
J. Investig. Dermatol. Symp. Proc. 10:21-30(2005).
[16]
VARIANTS PC3 PRO-164; ASP-171; SER-171; TYR-171; ASN-172 DEL; CYS-174;
ARG-469; PRO-469 AND LYS-472.
PubMed=17719747; DOI=10.1016/j.jdermsci.2007.07.003;
Liao H., Sayers J.M., Wilson N.J., Irvine A.D., Mellerio J.E.,
Baselga E., Bayliss S.J., Uliana V., Fimiani M., Lane E.B.,
McLean W.H., Leachman S.A., Smith F.J.;
"A spectrum of mutations in keratins K6a, K16 and K17 causing
pachyonychia congenita.";
J. Dermatol. Sci. 48:199-205(2007).
[17]
VARIANT PC3 GLN-468.
PubMed=17309457; DOI=10.1111/j.1468-3083.2006.01930.x;
Zhou H.L., Yang S., Gao M., Zhao X.Y., Zhu Y.G., Li W., Ren Y.Q.,
Liang Y.H., Du W.H., Zhang X.J.;
"A novel missense mutation L468Q of keratin 6a in pachyonychia
congenita type 1.";
J. Eur. Acad. Dermatol. Venereol. 21:351-355(2007).
[18]
VARIANTS PC3 ASP-171 AND HIS-465.
PubMed=18489596; DOI=10.1111/j.1365-2133.2008.08603.x;
Bai Z.L., Feng Y.G., Tan S.S., Wang X.Y., Xiao S.X., Wang H.,
Jia H.Q., Wu J.W., He D.L., Kang R.H.;
"Mutations of KRT6A are more frequent than those of KRT16 in
pachyonychia congenita type 1: report of a novel and a recently
reported mutation in two unrelated Chinese families.";
Br. J. Dermatol. 159:238-240(2008).
[19]
VARIANTS PC3 PRO-166; LYS-171; ASN-172 DEL; SER-174; ASN-178; PRO-463
AND SER-465.
PubMed=19416275; DOI=10.1111/j.1365-2133.2009.09062.x;
Lv Y.M., Yang S., Zhang Z., Cui Y., Quan C., Zhou F.S., Fang Q.Y.,
Du W.H., Zhang F.R., Chang J.M., Tao X.P., Zhang A.L., Kang R.H.,
Du W.D., Zhang X.J.;
"Novel and recurrent keratin 6A (KRT6A) mutations in Chinese patients
with pachyonychia congenita type 1.";
Br. J. Dermatol. 160:1327-1329(2009).
[20]
VARIANTS PC3 SER-171; LYS-171; ASN-172 DEL AND PRO-468.
PubMed=21326300; DOI=10.1038/jid.2011.20;
Wilson N.J., Leachman S.A., Hansen C.D., McMullan A.C., Milstone L.M.,
Schwartz M.E., McLean W.H., Hull P.R., Smith F.J.;
"A large mutational study in pachyonychia congenita.";
J. Invest. Dermatol. 131:1018-1024(2011).
-!- FUNCTION: Epidermis-specific type I keratin involved in wound
healing. Involved in the activation of follicular keratinocytes
after wounding, while it does not play a major role in
keratinocyte proliferation or migration. Participates in the
regulation of epithelial migration by inhibiting the activity of
SRC during wound repair. {ECO:0000250|UniProtKB:P50446}.
-!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT6
isomers associate with KRT16 and/or KRT17 (By similarity).
Interacts with TCHP (PubMed:15731013).
{ECO:0000250|UniProtKB:P50446, ECO:0000269|PubMed:15731013}.
-!- INTERACTION:
Q15834:CCDC85B; NbExp=2; IntAct=EBI-702198, EBI-739674;
Q08379:GOLGA2; NbExp=6; IntAct=EBI-702198, EBI-618309;
O14964:HGS; NbExp=3; IntAct=EBI-702198, EBI-740220;
F5H3M2:KIFC3; NbExp=4; IntAct=EBI-702198, EBI-11953930;
Q9BVG8:KIFC3; NbExp=5; IntAct=EBI-702198, EBI-2125614;
A1A4E9:KRT13; NbExp=5; IntAct=EBI-702198, EBI-10171552;
P13646:KRT13; NbExp=5; IntAct=EBI-702198, EBI-1223876;
P19012:KRT15; NbExp=10; IntAct=EBI-702198, EBI-739566;
Q7Z3Y9:KRT26; NbExp=4; IntAct=EBI-702198, EBI-12084444;
Q15323:KRT31; NbExp=11; IntAct=EBI-702198, EBI-948001;
O76015:KRT38; NbExp=9; IntAct=EBI-702198, EBI-1047263;
Q6A162:KRT40; NbExp=10; IntAct=EBI-702198, EBI-10171697;
O43765:SGTA; NbExp=3; IntAct=EBI-702198, EBI-347996;
Q9UBB9:TFIP11; NbExp=8; IntAct=EBI-702198, EBI-1105213;
P36406:TRIM23; NbExp=8; IntAct=EBI-702198, EBI-740098;
Q9BYV2:TRIM54; NbExp=9; IntAct=EBI-702198, EBI-2130429;
-!- TISSUE SPECIFICITY: Constitutively expressed in distinct types of
epithelia such as those in oral mucosa, esophagus, papillae of
tongue and hair follicle outer root sheath.
-!- DISEASE: Pachyonychia congenita 3 (PC3) [MIM:615726]: An autosomal
dominant genodermatosis characterized by hypertrophic nail
dystrophy, painful and highly debilitating plantar keratoderma,
oral leukokeratosis, and a variety of epidermal cysts.
{ECO:0000269|PubMed:10232400, ECO:0000269|PubMed:11886499,
ECO:0000269|PubMed:15387942, ECO:0000269|PubMed:15840119,
ECO:0000269|PubMed:16250206, ECO:0000269|PubMed:17309457,
ECO:0000269|PubMed:17719747, ECO:0000269|PubMed:18489596,
ECO:0000269|PubMed:19416275, ECO:0000269|PubMed:21326300,
ECO:0000269|PubMed:22668561, ECO:0000269|PubMed:7545493}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE from
atopic dermatitis (AD) patients. Identified as an IgE autoantigen
in atopic dermatitis (AD) patients with severe skin
manifestations.
-!- MISCELLANEOUS: There are at least six isoforms of human type II
keratin-6 (K6), K6A being the most abundant representing about 77%
of all forms found in epithelia.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin, I (acidic) and II (neutral to basic) (40-
55 and 56-70 kDa, respectively).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
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EMBL; L42583; AAC41767.1; -; Genomic_DNA.
EMBL; L42575; AAC41767.1; JOINED; Genomic_DNA.
EMBL; L42576; AAC41767.1; JOINED; Genomic_DNA.
EMBL; L42577; AAC41767.1; JOINED; Genomic_DNA.
EMBL; L42578; AAC41767.1; JOINED; Genomic_DNA.
EMBL; L42579; AAC41767.1; JOINED; Genomic_DNA.
EMBL; L42580; AAC41767.1; JOINED; Genomic_DNA.
EMBL; L42581; AAC41767.1; JOINED; Genomic_DNA.
EMBL; AH005420; AAB60696.1; -; Genomic_DNA.
EMBL; BT006899; AAP35545.1; -; mRNA.
EMBL; BC008807; AAH08807.1; -; mRNA.
EMBL; BC014152; AAH14152.1; -; mRNA.
EMBL; BC069269; AAH69269.1; -; mRNA.
EMBL; BC125058; AAI25059.1; -; mRNA.
EMBL; BC139753; AAI39754.1; -; mRNA.
EMBL; V01516; CAA24760.1; -; Genomic_DNA.
PIR; A57398; KRHUEA.
PIR; I61769; I61769.
RefSeq; NP_005545.1; NM_005554.3.
UniGene; Hs.700779; -.
PDB; 5KI0; NMR; -; A=533-551.
PDBsum; 5KI0; -.
ProteinModelPortal; P02538; -.
SMR; P02538; -.
BioGrid; 110051; 45.
DIP; DIP-533N; -.
IntAct; P02538; 42.
STRING; 9606.ENSP00000369317; -.
Allergome; 3326; Hom s 5.0101.
Allergome; 415; Hom s 5.
iPTMnet; P02538; -.
PhosphoSitePlus; P02538; -.
SwissPalm; P02538; -.
BioMuta; KRT6A; -.
DMDM; 1346344; -.
PaxDb; P02538; -.
PeptideAtlas; P02538; -.
PRIDE; P02538; -.
TopDownProteomics; P02538; -.
DNASU; 3853; -.
Ensembl; ENST00000330722; ENSP00000369317; ENSG00000205420.
GeneID; 3853; -.
KEGG; hsa:3853; -.
UCSC; uc001sam.4; human.
CTD; 3853; -.
DisGeNET; 3853; -.
EuPathDB; HostDB:ENSG00000205420.10; -.
GeneCards; KRT6A; -.
GeneReviews; KRT6A; -.
HGNC; HGNC:6443; KRT6A.
HPA; HPA045697; -.
HPA; HPA061168; -.
MalaCards; KRT6A; -.
MIM; 148041; gene.
MIM; 615726; phenotype.
neXtProt; NX_P02538; -.
OpenTargets; ENSG00000205420; -.
Orphanet; 2309; Pachyonychia congenita.
PharmGKB; PA30231; -.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; P02538; -.
KO; K07605; -.
OMA; MQDQVED; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P02538; -.
TreeFam; TF317854; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
ChiTaRS; KRT6A; human.
GeneWiki; Keratin_6A; -.
GenomeRNAi; 3853; -.
PRO; PR:P02538; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000205420; -.
CleanEx; HS_KRT6A; -.
ExpressionAtlas; P02538; baseline and differential.
Genevisible; P02538; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0045095; C:keratin filament; IEA:InterPro.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0051801; P:cytolysis in other organism involved in symbiotic interaction; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0002009; P:morphogenesis of an epithelium; ISS:UniProtKB.
GO; GO:0001899; P:negative regulation of cytolysis by symbiont of host cells; IDA:UniProtKB.
GO; GO:2000536; P:negative regulation of entry of bacterium into host cell; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; NAS:UniProtKB.
GO; GO:0042060; P:wound healing; ISS:UniProtKB.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allergen; Coiled coil; Complete proteome;
Direct protein sequencing; Disease mutation; Ectodermal dysplasia;
Intermediate filament; Keratin; Palmoplantar keratoderma;
Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.4}.
CHAIN 2 564 Keratin, type II cytoskeletal 6A.
/FTId=PRO_0000063731.
REGION 2 162 Head.
REGION 163 472 Rod.
REGION 163 198 Coil 1A.
REGION 199 217 Linker 1.
REGION 218 309 Coil 1B.
REGION 310 333 Linker 12.
REGION 334 472 Coil 2.
REGION 473 564 Tail.
SITE 414 414 Stutter.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.4}.
VARIANT 21 21 N -> S (in dbSNP:rs17845411).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_021264.
VARIANT 111 111 G -> D (in dbSNP:rs681063).
/FTId=VAR_035030.
VARIANT 164 164 R -> P (in PC3; dbSNP:rs62635293).
{ECO:0000269|PubMed:17719747}.
/FTId=VAR_072446.
VARIANT 166 166 Q -> P (in PC3; dbSNP:rs267607460).
{ECO:0000269|PubMed:19416275}.
/FTId=VAR_072447.
VARIANT 167 167 I -> N (in PC3; dbSNP:rs57126929).
{ECO:0000269|PubMed:16250206}.
/FTId=VAR_072448.
VARIANT 170 170 L -> F (in PC3; dbSNP:rs57448541).
{ECO:0000269|PubMed:16250206}.
/FTId=VAR_072449.
VARIANT 171 171 N -> D (in PC3; dbSNP:rs62635294).
{ECO:0000269|PubMed:17719747,
ECO:0000269|PubMed:18489596}.
/FTId=VAR_072450.
VARIANT 171 171 N -> K (in PC3; dbSNP:rs59685571).
{ECO:0000269|PubMed:10232400,
ECO:0000269|PubMed:16250206,
ECO:0000269|PubMed:19416275,
ECO:0000269|PubMed:21326300}.
/FTId=VAR_072451.
VARIANT 171 171 N -> S (in PC3; dbSNP:rs58556099).
{ECO:0000269|PubMed:16250206,
ECO:0000269|PubMed:17719747,
ECO:0000269|PubMed:21326300}.
/FTId=VAR_072452.
VARIANT 171 171 N -> Y (in PC3; dbSNP:rs62635294).
{ECO:0000269|PubMed:17719747}.
/FTId=VAR_072453.
VARIANT 171 171 Missing (in PC3).
{ECO:0000269|PubMed:16250206,
ECO:0000269|PubMed:7545493}.
/FTId=VAR_003878.
VARIANT 172 172 Missing (in PC3).
{ECO:0000269|PubMed:17719747,
ECO:0000269|PubMed:19416275,
ECO:0000269|PubMed:21326300}.
/FTId=VAR_072454.
VARIANT 174 174 F -> C (in PC3; dbSNP:rs61145796).
{ECO:0000269|PubMed:17719747}.
/FTId=VAR_072455.
VARIANT 174 174 F -> S (in PC3; dbSNP:rs61145796).
{ECO:0000269|PubMed:10232400,
ECO:0000269|PubMed:16250206,
ECO:0000269|PubMed:19416275}.
/FTId=VAR_072456.
VARIANT 174 174 F -> V (in PC3; dbSNP:rs28933087).
{ECO:0000269|PubMed:11886499}.
/FTId=VAR_017075.
VARIANT 176 176 S -> P (in PC3; dbSNP:rs59642296).
{ECO:0000269|PubMed:16250206}.
/FTId=VAR_072457.
VARIANT 178 178 I -> N (in PC3; dbSNP:rs267607461).
{ECO:0000269|PubMed:19416275}.
/FTId=VAR_072458.
VARIANT 462 462 I -> N (in PC3; dbSNP:rs57629991).
{ECO:0000269|PubMed:16250206}.
/FTId=VAR_072459.
VARIANT 462 462 I -> S (in PC3; dbSNP:rs57629991).
{ECO:0000269|PubMed:15387942}.
/FTId=VAR_072460.
VARIANT 463 463 A -> P (in PC3; dbSNP:rs267607462).
{ECO:0000269|PubMed:19416275}.
/FTId=VAR_072461.
VARIANT 464 464 T -> P (in PC3; dbSNP:rs61293647).
{ECO:0000269|PubMed:15840119}.
/FTId=VAR_072462.
VARIANT 465 465 Y -> H (in PC3; dbSNP:rs267607463).
{ECO:0000269|PubMed:18489596}.
/FTId=VAR_072463.
VARIANT 465 465 Y -> S (in PC3).
{ECO:0000269|PubMed:19416275}.
/FTId=VAR_072464.
VARIANT 468 468 L -> P (in PC3; dbSNP:rs59018888).
{ECO:0000269|PubMed:16250206,
ECO:0000269|PubMed:21326300}.
/FTId=VAR_072465.
VARIANT 468 468 L -> Q (in PC3; dbSNP:rs59018888).
{ECO:0000269|PubMed:17309457}.
/FTId=VAR_072466.
VARIANT 469 469 L -> P (in PC3; dbSNP:rs57052654).
{ECO:0000269|PubMed:16250206,
ECO:0000269|PubMed:17719747}.
/FTId=VAR_072467.
VARIANT 469 469 L -> R (in PC3; dbSNP:rs57052654).
{ECO:0000269|PubMed:11886499,
ECO:0000269|PubMed:17719747}.
/FTId=VAR_017076.
VARIANT 472 472 E -> K (in PC3; dbSNP:rs60554162).
{ECO:0000269|PubMed:11886499,
ECO:0000269|PubMed:17719747}.
/FTId=VAR_017077.
CONFLICT 192 192 E -> D (in Ref. 1; AAB60696).
{ECO:0000305}.
CONFLICT 241 241 G -> N (in Ref. 1; AAB60696).
{ECO:0000305}.
CONFLICT 249 249 F -> L (in Ref. 1; AAB60696).
{ECO:0000305}.
CONFLICT 395 395 I -> S (in Ref. 5; CAA24760).
{ECO:0000305}.
CONFLICT 404 404 N -> S (in Ref. 1; AAB60696).
{ECO:0000305}.
CONFLICT 443 443 R -> W (in Ref. 3; AAH69269).
{ECO:0000305}.
CONFLICT 486 486 I -> V (in Ref. 1; AAB60696).
{ECO:0000305}.
HELIX 539 541 {ECO:0000244|PDB:5KI0}.
HELIX 547 549 {ECO:0000244|PDB:5KI0}.
SEQUENCE 564 AA; 60045 MW; 26708916C7DC923A CRC64;
MASTSTTIRS HSSSRRGFSA NSARLPGVSR SGFSSVSVSR SRGSGGLGGA CGGAGFGSRS
LYGLGGSKRI SIGGGSCAIS GGYGSRAGGS YGFGGAGSGF GFGGGAGIGF GLGGGAGLAG
GFGGPGFPVC PPGGIQEVTV NQSLLTPLNL QIDPTIQRVR AEEREQIKTL NNKFASFIDK
VRFLEQQNKV LETKWTLLQE QGTKTVRQNL EPLFEQYINN LRRQLDSIVG ERGRLDSELR
GMQDLVEDFK NKYEDEINKR TAAENEFVTL KKDVDAAYMN KVELQAKADT LTDEINFLRA
LYDAELSQMQ THISDTSVVL SMDNNRNLDL DSIIAEVKAQ YEEIAQRSRA EAESWYQTKY
EELQVTAGRH GDDLRNTKQE IAEINRMIQR LRSEIDHVKK QCANLQAAIA DAEQRGEMAL
KDAKNKLEGL EDALQKAKQD LARLLKEYQE LMNVKLALDV EIATYRKLLE GEECRLNGEG
VGQVNISVVQ STVSSGYGGA SGVGSGLGLG GGSSYSYGSG LGVGGGFSSS SGRAIGGGLS
SVGGGSSTIK YTTTSSSSRK SYKH


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