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K2C71_HUMAN
ID   K2C71_HUMAN             Reviewed;         523 AA.
AC   Q3SY84; B3KVC1; Q3SY85; Q96DU2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Keratin, type II cytoskeletal 71;
DE   AltName: Full=Cytokeratin-71;
DE            Short=CK-71;
DE   AltName: Full=Keratin-71;
DE            Short=K71;
DE   AltName: Full=Type II inner root sheath-specific keratin-K6irs1;
DE            Short=Keratin 6 irs;
DE            Short=hK6irs;
DE            Short=hK6irs1;
DE   AltName: Full=Type-II keratin Kb34;
GN   Name=KRT71; Synonyms=K6IRS1, KB34, KRT6IRS1;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Scalp;
RX   PubMed=11982755; DOI=10.1046/j.1523-1747.2002.01711.x;
RA   Langbein L., Rogers M.A., Praetzel S., Aoki N., Winter H., Schweizer J.;
RT   "A novel epithelial keratin, hK6irs1, is expressed differentially in all
RT   layers of the inner root sheath, including specialized huxley cells
RT   (Flugelzellen) of the human hair follicle.";
RL   J. Invest. Dermatol. 118:789-799(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-464.
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-464.
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   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=12648212; DOI=10.1046/j.1523-1747.2003.12087.x;
RA   Langbein L., Rogers M.A., Praetzel S., Winter H., Schweizer J.;
RT   "K6irs1, K6irs2, K6irs3, and K6irs4 represent the inner-root-sheath-
RT   specific type II epithelial keratins of the human hair follicle.";
RL   J. Invest. Dermatol. 120:512-522(2003).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=16874310; DOI=10.1038/sj.jid.5700494;
RA   Langbein L., Rogers M.A., Praetzel-Wunder S., Helmke B., Schirmacher P.,
RA   Schweizer J.;
RT   "K25 (K25irs1), K26 (K25irs2), K27 (K25irs3), and K28 (K25irs4) represent
RT   the type I inner root sheath keratins of the human hair follicle.";
RL   J. Invest. Dermatol. 126:2377-2386(2006).
RN   [8]
RP   IDENTIFICATION BY MASS 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).
RN   [9]
RP   FUNCTION, INVOLVEMENT IN HYPT13, VARIANT HYPT13 CYS-141, CHARACTERIZATION
RP   OF VARIANT HYPT13 CYS-141, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=22592156; DOI=10.1038/jid.2012.154;
RA   Fujimoto A., Farooq M., Fujikawa H., Inoue A., Ohyama M., Ehama R.,
RA   Nakanishi J., Hagihara M., Iwabuchi T., Aoki J., Ito M., Shimomura Y.;
RT   "A missense mutation within the helix initiation motif of the keratin K71
RT   gene underlies autosomal dominant woolly hair/hypotrichosis.";
RL   J. Invest. Dermatol. 132:2342-2349(2012).
CC   -!- FUNCTION: Plays a central role in hair formation. Essential component
CC       of keratin intermediate filaments in the inner root sheath (IRS) of the
CC       hair follicle. {ECO:0000269|PubMed:22592156}.
CC   -!- SUBUNIT: Heterodimer of a type I and a type II keratin. Associates with
CC       KRT16 and/or KRT17 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q3SY84; A1A4E9: KRT13; NbExp=3; IntAct=EBI-2952676, EBI-10171552;
CC       Q3SY84; P19012: KRT15; NbExp=6; IntAct=EBI-2952676, EBI-739566;
CC       Q3SY84; P08779: KRT16; NbExp=3; IntAct=EBI-2952676, EBI-356410;
CC       Q3SY84; P05783: KRT18; NbExp=3; IntAct=EBI-2952676, EBI-297888;
CC       Q3SY84; P08727: KRT19; NbExp=3; IntAct=EBI-2952676, EBI-742756;
CC       Q3SY84; Q2M2I5: KRT24; NbExp=5; IntAct=EBI-2952676, EBI-2952736;
CC       Q3SY84; Q7Z3Z0: KRT25; NbExp=5; IntAct=EBI-2952676, EBI-11980019;
CC       Q3SY84; Q7Z3Y9: KRT26; NbExp=3; IntAct=EBI-2952676, EBI-12084444;
CC       Q3SY84; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2952676, EBI-3044087;
CC       Q3SY84; Q7Z3Y7: KRT28; NbExp=5; IntAct=EBI-2952676, EBI-11980489;
CC       Q3SY84; Q15323: KRT31; NbExp=6; IntAct=EBI-2952676, EBI-948001;
CC       Q3SY84; Q14525: KRT33B; NbExp=3; IntAct=EBI-2952676, EBI-1049638;
CC       Q3SY84; O76011: KRT34; NbExp=3; IntAct=EBI-2952676, EBI-1047093;
CC       Q3SY84; Q92764: KRT35; NbExp=3; IntAct=EBI-2952676, EBI-1058674;
CC       Q3SY84; O76014: KRT37; NbExp=3; IntAct=EBI-2952676, EBI-1045716;
CC       Q3SY84; O76015: KRT38; NbExp=6; IntAct=EBI-2952676, EBI-1047263;
CC       Q3SY84; Q6A162: KRT40; NbExp=6; IntAct=EBI-2952676, EBI-10171697;
CC       Q3SY84; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-2952676, EBI-739895;
CC       Q3SY84; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-2952676, EBI-712969;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:22592156}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in hair follicles from scalp.
CC       Specifically expressed in the inner root sheath (IRS) of the hair
CC       follicle. Present in the all 3 IRS layers: the cuticle, the Henle and
CC       the Huxley layers. Also detected in the pseudopods of specialized
CC       Huxley cells, termed Fluegelzellen, along the area of differentiated
CC       Henle cells (at protein level). {ECO:0000269|PubMed:11982755,
CC       ECO:0000269|PubMed:12648212, ECO:0000269|PubMed:16874310,
CC       ECO:0000269|PubMed:22592156}.
CC   -!- DEVELOPMENTAL STAGE: In all 3 IRS layers, expression begins
CC       simultaneously in adjacent cells of the lowermost bulb above the
CC       germinative cell pool and terminated higher up in the follicle with the
CC       asynchronous terminal differentiation of each cell layer (at protein
CC       level).
CC   -!- DISEASE: Hypotrichosis 13 (HYPT13) [MIM:615896]: A form of
CC       hypotrichosis, a condition characterized by the presence of less than
CC       the normal amount of hair and abnormal hair follicles and shafts, which
CC       are thin and atrophic. The extent of scalp and body hair involvement
CC       can be very variable, within as well as between families. HYPT13 is an
CC       autosomal dominant form characterized by sparse woolly hair.
CC       {ECO:0000269|PubMed:22592156}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC       respectively).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AJ308599; CAC43429.1; -; mRNA.
DR   EMBL; AK122795; BAG53733.1; -; mRNA.
DR   EMBL; AC055736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW96636.1; -; Genomic_DNA.
DR   EMBL; BC103917; AAI03918.1; -; mRNA.
DR   EMBL; BC103918; AAI03919.1; -; mRNA.
DR   CCDS; CCDS8831.1; -.
DR   RefSeq; NP_258259.1; NM_033448.2.
DR   AlphaFoldDB; Q3SY84; -.
DR   SMR; Q3SY84; -.
DR   BioGRID; 125205; 28.
DR   ComplexPortal; CPX-5665; Keratin-25 - Keratin-71 dimer complex.
DR   IntAct; Q3SY84; 29.
DR   STRING; 9606.ENSP00000267119; -.
DR   GlyGen; Q3SY84; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3SY84; -.
DR   PhosphoSitePlus; Q3SY84; -.
DR   SwissPalm; Q3SY84; -.
DR   BioMuta; KRT71; -.
DR   DMDM; 296439318; -.
DR   EPD; Q3SY84; -.
DR   jPOST; Q3SY84; -.
DR   MassIVE; Q3SY84; -.
DR   PaxDb; Q3SY84; -.
DR   PeptideAtlas; Q3SY84; -.
DR   PRIDE; Q3SY84; -.
DR   ProteomicsDB; 61847; -.
DR   Antibodypedia; 26633; 99 antibodies from 18 providers.
DR   DNASU; 112802; -.
DR   Ensembl; ENST00000267119.6; ENSP00000267119.5; ENSG00000139648.7.
DR   GeneID; 112802; -.
DR   KEGG; hsa:112802; -.
DR   MANE-Select; ENST00000267119.6; ENSP00000267119.5; NM_033448.3; NP_258259.1.
DR   UCSC; uc001sao.3; human.
DR   CTD; 112802; -.
DR   DisGeNET; 112802; -.
DR   GeneCards; KRT71; -.
DR   HGNC; HGNC:28927; KRT71.
DR   HPA; ENSG00000139648; Tissue enriched (skin).
DR   MalaCards; KRT71; -.
DR   MIM; 608245; gene.
DR   MIM; 615896; phenotype.
DR   neXtProt; NX_Q3SY84; -.
DR   OpenTargets; ENSG00000139648; -.
DR   Orphanet; 170; Woolly hair.
DR   PharmGKB; PA147357697; -.
DR   VEuPathDB; HostDB:ENSG00000139648; -.
DR   eggNOG; ENOG502SK67; Eukaryota.
DR   GeneTree; ENSGT00940000162089; -.
DR   HOGENOM; CLU_012560_6_1_1; -.
DR   InParanoid; Q3SY84; -.
DR   OMA; GPVCSTV; -.
DR   OrthoDB; 671547at2759; -.
DR   PhylomeDB; Q3SY84; -.
DR   TreeFam; TF317854; -.
DR   PathwayCommons; Q3SY84; -.
DR   Reactome; R-HSA-6805567; Keratinization.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   SignaLink; Q3SY84; -.
DR   BioGRID-ORCS; 112802; 18 hits in 1074 CRISPR screens.
DR   GenomeRNAi; 112802; -.
DR   Pharos; Q3SY84; Tbio.
DR   PRO; PR:Q3SY84; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q3SY84; protein.
DR   Bgee; ENSG00000139648; Expressed in upper arm skin and 53 other tissues.
DR   Genevisible; Q3SY84; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
DR   GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:UniProtKB.
DR   GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
DR   GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Hypotrichosis;
KW   Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..523
FT                   /note="Keratin, type II cytoskeletal 71"
FT                   /id="PRO_0000314874"
FT   DOMAIN          130..443
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..129
FT                   /note="Head"
FT   REGION          130..165
FT                   /note="Coil 1A"
FT   REGION          166..184
FT                   /note="Linker 1"
FT   REGION          185..276
FT                   /note="Coil 1B"
FT   REGION          277..300
FT                   /note="Linker 12"
FT   REGION          301..439
FT                   /note="Coil 2"
FT   REGION          440..523
FT                   /note="Tail"
FT   REGION          492..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            381
FT                   /note="Stutter"
FT   VARIANT         107
FT                   /note="V -> I (in dbSNP:rs665522)"
FT                   /id="VAR_038082"
FT   VARIANT         122
FT                   /note="E -> K (in dbSNP:rs665470)"
FT                   /id="VAR_038083"
FT   VARIANT         141
FT                   /note="F -> C (in HYPT13; dominant negative; decreased
FT                   keratin intermediate filament formation;
FT                   dbSNP:rs587777545)"
FT                   /evidence="ECO:0000269|PubMed:22592156"
FT                   /id="VAR_071406"
FT   VARIANT         355
FT                   /note="I -> F (in dbSNP:rs35988863)"
FT                   /id="VAR_038084"
FT   VARIANT         464
FT                   /note="V -> G (in dbSNP:rs10783518)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT                   /id="VAR_038085"
FT   VARIANT         523
FT                   /note="R -> Q (in dbSNP:rs2292506)"
FT                   /id="VAR_038086"
FT   CONFLICT        210
FT                   /note="R -> Q (in Ref. 5; AAI03919)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   523 AA;  57292 MW;  797F5655EE3A62D7 CRC64;
     MSRQFTCKSG AAAKGGFSGC SAVLSGGSSS SFRAGSKGLS GGFGSRSLYS LGGVRSLNVA
     SGSGKSGGYG FGRGRASGFA GSMFGSVALG PVCPTVCPPG GIHQVTVNES LLAPLNVELD
     PEIQKVRAQE REQIKALNNK FASFIDKVRF LEQQNQVLET KWELLQQLDL NNCKNNLEPI
     LEGYISNLRK QLETLSGDRV RLDSELRNVR DVVEDYKKRY EEEINKRTAA ENEFVLLKKD
     VDAAYANKVE LQAKVESMDQ EIKFFRCLFE AEITQIQSHI SDMSVILSMD NNRNLDLDSI
     IDEVRTQYEE IALKSKAEAE ALYQTKFQEL QLAAGRHGDD LKNTKNEISE LTRLIQRIRS
     EIENVKKQAS NLETAIADAE QRGDNALKDA RAKLDELEGA LHQAKEELAR MLREYQELMS
     LKLALDMEIA TYRKLLESEE CRMSGEFPSP VSISIISSTS GGSVYGFRPS MVSGGYVANS
     SNCISGVCSV RGGEGRSRGS ANDYKDTLGK GSSLSAPSKK TSR
 
 
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