ANKH_HUMAN
ID ANKH_HUMAN Reviewed; 492 AA.
AC Q9HCJ1; B2RCA7; B3KMG4; D3DTD4; Q9NQW2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Progressive ankylosis protein homolog;
DE Short=ANK;
GN Name=ANKH; Synonyms=KIAA1581; ORFNames=UNQ241/PRO274;
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] (ISOFORM 1).
RX PubMed=10894769; DOI=10.1126/science.289.5477.265;
RA Ho A.M., Johnson M.D., Kingsley D.M.;
RT "Role of the mouse ank gene in control of tissue calcification and
RT arthritis.";
RL Science 289:265-270(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Ovarian cancer;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [8]
RP VARIANTS CMDD SER-375 DEL; PHE-376 DEL AND ALA-380 INS.
RX PubMed=11326338; DOI=10.1086/320612;
RA Reichenberger E., Tiziani V., Watanabe S., Park L., Ueki Y., Santanna C.,
RA Baur S.T., Shiang R., Grange D.K., Beighton P., Gardner J., Hamersma H.,
RA Sellars S., Ramesar R., Lidral A.C., Sommer A., Raposo do Amaral C.M.,
RA Gorlin R.J., Mulliken J.B., Olsen B.R.;
RT "Autosomal dominant craniometaphyseal dysplasia is caused by mutations in
RT the transmembrane protein ANK.";
RL Am. J. Hum. Genet. 68:1321-1326(2001).
RN [9]
RP VARIANTS CMDD ARG-292; ARG-331; SER-375 DEL; PHE-377 DEL; ALA-380 INS AND
RP ARG-389.
RX PubMed=11326272; DOI=10.1038/ng0501-37;
RA Nuernberg P., Thiele H., Chandler D., Hoehne W., Cunningham M.L.,
RA Ritter H., Leschik G., Uhlmann K., Mischung C., Harrop K., Goldblatt J.,
RA Borochowitz Z.U., Kotzot D., Westermann F., Mundlos S., Braun H.-S.,
RA Laing N., Tinschert S.;
RT "Heterozygous mutations in ANKH, the human ortholog of the mouse
RT progressive ankylosis gene, result in craniometaphyseal dysplasia.";
RL Nat. Genet. 28:37-41(2001).
RN [10]
RP VARIANTS CCAL2 THR-48 AND GLU-490 DEL.
RX PubMed=12297987; DOI=10.1086/343054;
RA Pendleton A., Johnson M.D., Hughes A., Gurley K.A., Ho A.M., Doherty M.,
RA Dixey J., Gillet P., Loeuille D., McGrath R., Reginato A., Shiang R.,
RA Wright G., Netter P., Williams C., Kingsley D.M.;
RT "Mutations in ANKH cause chondrocalcinosis.";
RL Am. J. Hum. Genet. 71:933-940(2002).
RN [11]
RP VARIANT CCAL2 LEU-5.
RX PubMed=12297989; DOI=10.1086/343053;
RA Williams C.J., Zhang Y., Timms A., Bonavita G., Caeiro F., Broxholme J.,
RA Cuthbertson J., Jones Y., Marchegiani R., Reginato A., Russell R.G.G.,
RA Wordsworth B.P., Carr A.J., Brown M.A.;
RT "Autosomal dominant familial calcium pyrophosphate dihydrate deposition
RT disease is caused by mutation in the transmembrane protein ANKH.";
RL Am. J. Hum. Genet. 71:985-991(2002).
RN [12]
RP VARIANT CCAL2 THR-5.
RX PubMed=13130483; DOI=10.1002/art.11133;
RA Williams C.J., Pendleton A., Bonavita G., Reginato A.J., Hughes A.E.,
RA Peariso S., Doherty M., McCarty D.J., Ryan L.M.;
RT "Mutations in the amino terminus of ANKH in two US families with calcium
RT pyrophosphate dihydrate crystal deposition disease.";
RL Arthritis Rheum. 48:2627-2631(2003).
CC -!- FUNCTION: Regulates intra- and extracellular levels of inorganic
CC pyrophosphate (PPi), probably functioning as PPi transporter.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HCJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCJ1-2; Sequence=VSP_055824;
CC -!- TISSUE SPECIFICITY: Found in osteoblasts from mandibular bone and from
CC iliac bone; not detected in osteoclastic cells.
CC -!- DISEASE: Chondrocalcinosis 2 (CCAL2) [MIM:118600]: Chondrocalcinosis is
CC a common cause of joint pain and arthritis caused by calcium deposition
CC in articular cartilage and the presence of calcium hypophosphate
CC crystals in synovial fluid, cartilage and periarticular soft tissue.
CC CCAL2 inheritance is autosomal dominant. {ECO:0000269|PubMed:12297987,
CC ECO:0000269|PubMed:12297989, ECO:0000269|PubMed:13130483}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Craniometaphyseal dysplasia, autosomal dominant (CMDD)
CC [MIM:123000]: An osteochondrodysplasia characterized by hyperostosis
CC and sclerosis of the craniofacial bones associated with abnormal
CC modeling of the metaphyses. Sclerosis of the skull may lead to
CC asymmetry of the mandible, as well as to cranial nerve compression,
CC that may finally result in hearing loss and facial palsy.
CC {ECO:0000269|PubMed:11326272, ECO:0000269|PubMed:11326338}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ANKH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13407.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF274753; AAF88039.1; -; mRNA.
DR EMBL; AB046801; BAB13407.1; ALT_INIT; mRNA.
DR EMBL; AY358503; AAQ88867.1; -; mRNA.
DR EMBL; AK001799; BAG50976.1; -; mRNA.
DR EMBL; AC010491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK315012; BAG37504.1; -; mRNA.
DR EMBL; CH471102; EAX08034.1; -; Genomic_DNA.
DR EMBL; CH471102; EAX08035.1; -; Genomic_DNA.
DR EMBL; BC009835; AAH09835.1; -; mRNA.
DR EMBL; BC014526; AAH14526.1; -; mRNA.
DR CCDS; CCDS3885.1; -. [Q9HCJ1-1]
DR RefSeq; NP_473368.1; NM_054027.4. [Q9HCJ1-1]
DR AlphaFoldDB; Q9HCJ1; -.
DR SMR; Q9HCJ1; -.
DR BioGRID; 121103; 15.
DR IntAct; Q9HCJ1; 1.
DR STRING; 9606.ENSP00000284268; -.
DR TCDB; 2.A.66.9.1; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR iPTMnet; Q9HCJ1; -.
DR PhosphoSitePlus; Q9HCJ1; -.
DR BioMuta; ANKH; -.
DR DMDM; 17366849; -.
DR EPD; Q9HCJ1; -.
DR jPOST; Q9HCJ1; -.
DR MassIVE; Q9HCJ1; -.
DR MaxQB; Q9HCJ1; -.
DR PaxDb; Q9HCJ1; -.
DR PeptideAtlas; Q9HCJ1; -.
DR PRIDE; Q9HCJ1; -.
DR ProteomicsDB; 3485; -.
DR ProteomicsDB; 81736; -. [Q9HCJ1-1]
DR Antibodypedia; 43269; 117 antibodies from 24 providers.
DR DNASU; 56172; -.
DR Ensembl; ENST00000284268.8; ENSP00000284268.6; ENSG00000154122.14. [Q9HCJ1-1]
DR GeneID; 56172; -.
DR KEGG; hsa:56172; -.
DR MANE-Select; ENST00000284268.8; ENSP00000284268.6; NM_054027.6; NP_473368.1.
DR UCSC; uc003jfm.5; human. [Q9HCJ1-1]
DR CTD; 56172; -.
DR DisGeNET; 56172; -.
DR GeneCards; ANKH; -.
DR GeneReviews; ANKH; -.
DR HGNC; HGNC:15492; ANKH.
DR HPA; ENSG00000154122; Low tissue specificity.
DR MalaCards; ANKH; -.
DR MIM; 118600; phenotype.
DR MIM; 123000; phenotype.
DR MIM; 605145; gene.
DR neXtProt; NX_Q9HCJ1; -.
DR OpenTargets; ENSG00000154122; -.
DR Orphanet; 1522; Craniometaphyseal dysplasia.
DR Orphanet; 1416; Familial calcium pyrophosphate deposition.
DR PharmGKB; PA24801; -.
DR VEuPathDB; HostDB:ENSG00000154122; -.
DR eggNOG; ENOG502QWCU; Eukaryota.
DR GeneTree; ENSGT00390000012189; -.
DR HOGENOM; CLU_044298_0_0_1; -.
DR InParanoid; Q9HCJ1; -.
DR OMA; RRFYQGI; -.
DR OrthoDB; 484099at2759; -.
DR PhylomeDB; Q9HCJ1; -.
DR TreeFam; TF333504; -.
DR PathwayCommons; Q9HCJ1; -.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR SignaLink; Q9HCJ1; -.
DR SIGNOR; Q9HCJ1; -.
DR BioGRID-ORCS; 56172; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; ANKH; human.
DR GeneWiki; ANKH; -.
DR GenomeRNAi; 56172; -.
DR Pharos; Q9HCJ1; Tbio.
DR PRO; PR:Q9HCJ1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9HCJ1; protein.
DR Bgee; ENSG00000154122; Expressed in tibia and 180 other tissues.
DR ExpressionAtlas; Q9HCJ1; baseline and differential.
DR Genevisible; Q9HCJ1; HS.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0019867; C:outer membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030504; F:inorganic diphosphate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0071529; P:cementum mineralization; IEA:Ensembl.
DR GO; GO:0071344; P:diphosphate metabolic process; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; NAS:UniProtKB.
DR GO; GO:0055062; P:phosphate ion homeostasis; IEA:Ensembl.
DR GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:1904383; P:response to sodium phosphate; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; NAS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR InterPro; IPR009887; ANKH.
DR PANTHER; PTHR28384; PTHR28384; 1.
DR Pfam; PF07260; ANKH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Deafness; Disease variant; Membrane;
KW Phosphate transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..492
FT /note="Progressive ankylosis protein homolog"
FT /id="PRO_0000137467"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 458..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055824"
FT VARIANT 5
FT /note="P -> L (in CCAL2; dbSNP:rs121908409)"
FT /evidence="ECO:0000269|PubMed:12297989"
FT /id="VAR_022606"
FT VARIANT 5
FT /note="P -> T (in CCAL2; dbSNP:rs121908410)"
FT /evidence="ECO:0000269|PubMed:13130483"
FT /id="VAR_022607"
FT VARIANT 48
FT /note="M -> T (in CCAL2; dbSNP:rs121908407)"
FT /evidence="ECO:0000269|PubMed:12297987"
FT /id="VAR_017556"
FT VARIANT 292
FT /note="W -> R (in CMDD)"
FT /evidence="ECO:0000269|PubMed:11326272"
FT /id="VAR_012192"
FT VARIANT 331
FT /note="C -> R (in CMDD)"
FT /evidence="ECO:0000269|PubMed:11326272"
FT /id="VAR_012193"
FT VARIANT 375
FT /note="Missing (in CMDD)"
FT /evidence="ECO:0000269|PubMed:11326272,
FT ECO:0000269|PubMed:11326338"
FT /id="VAR_012194"
FT VARIANT 376
FT /note="Missing (in CMDD)"
FT /evidence="ECO:0000269|PubMed:11326338"
FT /id="VAR_012195"
FT VARIANT 377
FT /note="Missing (in CMDD; dbSNP:rs121908405)"
FT /evidence="ECO:0000269|PubMed:11326272"
FT /id="VAR_012196"
FT VARIANT 380
FT /note="P -> PA (in CMDD)"
FT /evidence="ECO:0000269|PubMed:11326272,
FT ECO:0000269|PubMed:11326338"
FT /id="VAR_012197"
FT VARIANT 389
FT /note="G -> R (in CMDD; dbSNP:rs28939080)"
FT /evidence="ECO:0000269|PubMed:11326272"
FT /id="VAR_012198"
FT VARIANT 490
FT /note="Missing (in CCAL2; sporadic; dbSNP:rs121908408)"
FT /evidence="ECO:0000269|PubMed:12297987"
FT /id="VAR_017557"
FT CONFLICT 78
FT /note="N -> S (in Ref. 1; AAF88039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 54241 MW; 44BFEE9089BDEC6B CRC64;
MVKFPALTHY WPLIRFLVPL GITNIAIDFG EQALNRGIAA VKEDAVEMLA SYGLAYSLMK
FFTGPMSDFK NVGLVFVNSK RDRTKAVLCM VVAGAIAAVF HTLIAYSDLG YYIINKLHHV
DESVGSKTRR AFLYLAAFPF MDAMAWTHAG ILLKHKYSFL VGCASISDVI AQVVFVAILL
HSHLECREPL LIPILSLYMG ALVRCTTLCL GYYKNIHDII PDRSGPELGG DATIRKMLSF
WWPLALILAT QRISRPIVNL FVSRDLGGSS AATEAVAILT ATYPVGHMPY GWLTEIRAVY
PAFDKNNPSN KLVSTSNTVT AAHIKKFTFV CMALSLTLCF VMFWTPNVSE KILIDIIGVD
FAFAELCVVP LRIFSFFPVP VTVRAHLTGW LMTLKKTFVL APSSVLRIIV LIASLVVLPY
LGVHGATLGV GSLLAGFVGE STMVAIAACY VYRKQKKKME NESATEGEDS AMTDMPPTEE
VTDIVEMREE NE
