ID   K22O_HUMAN              Reviewed;         638 AA.
AC   Q01546; B4DRR3; Q7Z795;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   24-JAN-2024, entry version 184.
DE   RecName: Full=Keratin, type II cytoskeletal 2 oral;
DE   AltName: Full=Cytokeratin-2P;
DE            Short=CK-2P;
DE            Short=K2P;
DE   AltName: Full=Keratin-76;
DE            Short=K76;
DE   AltName: Full=Type-II keratin Kb9;
GN   Name=KRT76; Synonyms=KRT2B, KRT2P;
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], FUNCTION, DEVELOPMENTAL STAGE, AND VARIANT
RP   THR-359.
RX   PubMed=1282112; DOI=10.1111/j.1432-0436.1992.tb00690.x;
RA   Collin C., Ouhayoun J.P., Grund C., Franke W.W.;
RT   "Suprabasal marker proteins distinguishing keratinizing squamous epithelia:
RT   cytokeratin 2 polypeptides of oral masticatory epithelium and epidermis are
RT   different.";
RL   Differentiation 51:137-148(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15737194; DOI=10.1111/j.0022-202x.2004.23530.x;
RA   Rogers M.A., Edler L., Winter H., Langbein L., Beckmann I., Schweizer J.;
RT   "Characterization of new members of the human type II keratin gene family
RT   and a general evaluation of the keratin gene domain on chromosome
RT   12q13.13.";
RL   J. Invest. Dermatol. 124:536-544(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [6]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-168.
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., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [7]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-359, AND IDENTIFICATION BY MASS
RP   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).
CC   -!- FUNCTION: Probably contributes to terminal cornification.
CC       {ECO:0000269|PubMed:1282112}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC   -!- INTERACTION:
CC       Q01546; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-2952745, EBI-8643161;
CC       Q01546; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-2952745, EBI-747505;
CC       Q01546; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-2952745, EBI-1383687;
CC       Q01546; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2952745, EBI-10961624;
CC       Q01546; Q16543: CDC37; NbExp=3; IntAct=EBI-2952745, EBI-295634;
CC       Q01546; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-2952745, EBI-749051;
CC       Q01546; Q6W0C5: DPPA3; NbExp=3; IntAct=EBI-2952745, EBI-12082590;
CC       Q01546; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-2952745, EBI-742102;
CC       Q01546; Q6PJQ5: FOXR2; NbExp=3; IntAct=EBI-2952745, EBI-8468543;
CC       Q01546; O43559: FRS3; NbExp=3; IntAct=EBI-2952745, EBI-725515;
CC       Q01546; O14964: HGS; NbExp=3; IntAct=EBI-2952745, EBI-740220;
CC       Q01546; Q9UI26-2: IPO11; NbExp=3; IntAct=EBI-2952745, EBI-12200335;
CC       Q01546; Q8NA54: IQUB; NbExp=3; IntAct=EBI-2952745, EBI-10220600;
CC       Q01546; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2952745, EBI-14069005;
CC       Q01546; P08779: KRT16; NbExp=3; IntAct=EBI-2952745, EBI-356410;
CC       Q01546; P35900: KRT20; NbExp=3; IntAct=EBI-2952745, EBI-742094;
CC       Q01546; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-2952745, EBI-11980019;
CC       Q01546; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2952745, EBI-3044087;
CC       Q01546; Q15323: KRT31; NbExp=5; IntAct=EBI-2952745, EBI-948001;
CC       Q01546; O76013-2: KRT36; NbExp=3; IntAct=EBI-2952745, EBI-11958506;
CC       Q01546; O76014: KRT37; NbExp=3; IntAct=EBI-2952745, EBI-1045716;
CC       Q01546; O76015: KRT38; NbExp=3; IntAct=EBI-2952745, EBI-1047263;
CC       Q01546; Q6A163: KRT39; NbExp=3; IntAct=EBI-2952745, EBI-11958242;
CC       Q01546; Q6A162: KRT40; NbExp=3; IntAct=EBI-2952745, EBI-10171697;
CC       Q01546; O95678: KRT75; NbExp=3; IntAct=EBI-2952745, EBI-2949715;
CC       Q01546; O43790: KRT86; NbExp=3; IntAct=EBI-2952745, EBI-9996498;
CC       Q01546; O95447: LCA5L; NbExp=3; IntAct=EBI-2952745, EBI-8473670;
CC       Q01546; P61968: LMO4; NbExp=3; IntAct=EBI-2952745, EBI-2798728;
CC       Q01546; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2952745, EBI-10172526;
CC       Q01546; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2952745, EBI-11522433;
CC       Q01546; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-2952745, EBI-10271199;
CC       Q01546; O15160: POLR1C; NbExp=5; IntAct=EBI-2952745, EBI-1055079;
CC       Q01546; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-2952745, EBI-748350;
CC       Q01546; Q63HR2: TNS2; NbExp=3; IntAct=EBI-2952745, EBI-949753;
CC       Q01546; P36406: TRIM23; NbExp=3; IntAct=EBI-2952745, EBI-740098;
CC       Q01546; P14373: TRIM27; NbExp=3; IntAct=EBI-2952745, EBI-719493;
CC       Q01546; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2952745, EBI-2130429;
CC       Q01546; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-2952745, EBI-744794;
CC       Q01546; Q8N720: ZNF655; NbExp=3; IntAct=EBI-2952745, EBI-625509;
CC   -!- DEVELOPMENTAL STAGE: Synthesized during maturation of epidermal
CC       keratinocytes. {ECO:0000269|PubMed:1282112}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG61375.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M99063; AAA35746.1; -; mRNA.
DR   EMBL; AJ564103; CAD91891.1; -; Genomic_DNA.
DR   EMBL; AK299390; BAG61375.1; ALT_SEQ; mRNA.
DR   EMBL; AC068988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC139763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS8838.1; -.
DR   PIR; I53169; I53169.
DR   RefSeq; NP_056932.2; NM_015848.4.
DR   AlphaFoldDB; Q01546; -.
DR   SMR; Q01546; -.
DR   BioGRID; 119492; 60.
DR   IntAct; Q01546; 53.
DR   MINT; Q01546; -.
DR   STRING; 9606.ENSP00000330101; -.
DR   iPTMnet; Q01546; -.
DR   PhosphoSitePlus; Q01546; -.
DR   SwissPalm; Q01546; -.
DR   BioMuta; KRT76; -.
DR   DMDM; 317373371; -.
DR   jPOST; Q01546; -.
DR   MassIVE; Q01546; -.
DR   PaxDb; 9606-ENSP00000330101; -.
DR   PeptideAtlas; Q01546; -.
DR   PRIDE; Q01546; -.
DR   ProteomicsDB; 57971; -.
DR   Antibodypedia; 14669; 696 antibodies from 24 providers.
DR   DNASU; 51350; -.
DR   Ensembl; ENST00000332411.2; ENSP00000330101.2; ENSG00000185069.2.
DR   GeneID; 51350; -.
DR   KEGG; hsa:51350; -.
DR   MANE-Select; ENST00000332411.2; ENSP00000330101.2; NM_015848.4; NP_056932.2.
DR   UCSC; uc001sax.3; human.
DR   AGR; HGNC:24430; -.
DR   CTD; 51350; -.
DR   DisGeNET; 51350; -.
DR   GeneCards; KRT76; -.
DR   HGNC; HGNC:24430; KRT76.
DR   HPA; ENSG00000185069; Group enriched (lymphoid tissue, salivary gland).
DR   MIM; 616671; gene.
DR   neXtProt; NX_Q01546; -.
DR   OpenTargets; ENSG00000185069; -.
DR   PharmGKB; PA147357785; -.
DR   VEuPathDB; HostDB:ENSG00000185069; -.
DR   eggNOG; ENOG502QURK; Eukaryota.
DR   GeneTree; ENSGT00940000162365; -.
DR   HOGENOM; CLU_012560_6_0_1; -.
DR   InParanoid; Q01546; -.
DR   OMA; MSHSGMG; -.
DR   OrthoDB; 4640531at2759; -.
DR   PhylomeDB; Q01546; -.
DR   TreeFam; TF317854; -.
DR   PathwayCommons; Q01546; -.
DR   Reactome; R-HSA-6805567; Keratinization.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   SignaLink; Q01546; -.
DR   BioGRID-ORCS; 51350; 11 hits in 1146 CRISPR screens.
DR   GenomeRNAi; 51350; -.
DR   Pharos; Q01546; Tdark.
DR   PRO; PR:Q01546; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q01546; Protein.
DR   Bgee; ENSG00000185069; Expressed in gingiva and 17 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
DR   GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR   GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR   GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR   GO; GO:0048733; P:sebaceous gland development; IEA:Ensembl.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45616:SF29; KERATIN, TYPE II CYTOSKELETAL 2 ORAL; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 3.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
DR   Genevisible; Q01546; HS.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin; Methylation;
KW   Reference proteome.
FT   CHAIN           1..638
FT                   /note="Keratin, type II cytoskeletal 2 oral"
FT                   /id="PRO_0000063714"
FT   DOMAIN          183..496
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..182
FT                   /note="Head"
FT   REGION          183..218
FT                   /note="Coil 1A"
FT   REGION          219..237
FT                   /note="Linker 1"
FT   REGION          238..329
FT                   /note="Coil 1B"
FT   REGION          330..353
FT                   /note="Linker 12"
FT   REGION          354..492
FT                   /note="Coil 2"
FT   REGION          493..638
FT                   /note="Tail"
FT   REGION          532..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         85
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT   MOD_RES         110
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT   MOD_RES         584
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT   VARIANT         168
FT                   /note="L -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036368"
FT   VARIANT         283
FT                   /note="A -> T (in dbSNP:rs11170271)"
FT                   /id="VAR_028425"
FT   VARIANT         359
FT                   /note="A -> T (in dbSNP:rs6580904)"
FT                   /evidence="ECO:0000269|PubMed:1282112,
FT                   ECO:0007744|PubMed:21269460"
FT                   /id="VAR_028426"
FT   VARIANT         629
FT                   /note="T -> M (in dbSNP:rs2280480)"
FT                   /id="VAR_028427"
FT   CONFLICT        356
FT                   /note="E -> K (in Ref. 3; BAG61375)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   638 AA;  65841 MW;  6A312B8260BE06A9 CRC64;
     MNRQVCKKSF SGRSQGFSGR SAVVSGSSRM SCVARSGGAG GGACGFRSGA GSFGSRSLYN
     LGSNKSISIS VAAGSSRAGG FGGGRSSCGF AGGYGGGFGG SYGGGFGGGR GVGSGFGGAG
     GFGGAGGFGG PGVFGGPGSF GGPGGFGPGG FPGGIQEVIV NQSLLQPLNV EIDPQIGQVK
     AQEREQIKTL NNKFASFIDK VRFLEQQNKV LETKWELLQQ QTTGSGPSSL EPCFESYISF
     LCKQLDSLLG ERGNLEGELK SMQDLVEDFK KKYEDEINKR TAAENEFVGL KKDVDAAFMN
     KVELQAKVDS LTDEVSFLRT LYEMELSQMQ SHASDTSVVL SMDNNRCLDL GSIIAEVRAQ
     YEEIAQRSKS EAEALYQTKL GELQTTAGRH GDDLRNTKSE IMELNRMIQR LRAEIENVKK
     QNANLQTAIA EAEQRGEMAL KDANAKLQDL QTALQKAKDD LARLLRDYQE LMNVKLALDV
     EIATYRKLLE GEECRMSGEC QSAVCISVVS NVTSTSGSSG SSRGVFGGVS GSGSGGYKGG
     SSSSSSSGYG VSGGSGSGYG GVSSGSTGGR GSSGSYQSSS SGSRLGGAGS ISVSHSGMGS
     SSGSIQTSGG SGYKSGGGGS TSIRFSQTTS SSQHSSTK
//