CNNM4_HUMAN
ID CNNM4_HUMAN Reviewed; 775 AA.
AC Q6P4Q7; B7Z1U0; C7SQM3; C7SQM4; C7SQM5; Q53RE5; Q9H9G3; Q9HCI0; Q9NRN1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Metal transporter CNNM4;
DE AltName: Full=Ancient conserved domain-containing protein 4;
DE AltName: Full=Cyclin-M4;
GN Name=CNNM4; Synonyms=ACDP4, KIAA1592;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 570-775 (ISOFORM 1).
RC TISSUE=Cerebellum, and Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-126.
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-467, VARIANTS JALIS GLN-236 AND
RP PRO-324, AND FUNCTION.
RX PubMed=19200527; DOI=10.1016/j.ajhg.2009.01.006;
RA Polok B., Escher P., Ambresin A., Chouery E., Bolay S., Meunier I., Nan F.,
RA Hamel C., Munier F.L., Thilo B., Megarbane A., Schorderet D.F.;
RT "Mutations in CNNM4 cause recessive cone-rod dystrophy with amelogenesis
RT imperfecta.";
RL Am. J. Hum. Genet. 84:259-265(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-775 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12657465; DOI=10.1016/s0378-1119(02)01210-6;
RA Wang C.-Y., Shi J.-D., Yang P., Kumar P.G., Li Q.-Z., Run Q.-G., Su Y.-C.,
RA Scott H.S., Kao K.-J., She J.-X.;
RT "Molecular cloning and characterization of a novel gene family of four
RT ancient conserved domain proteins (ACDP).";
RL Gene 306:37-44(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-775 (ISOFORM 1).
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 [7]
RP INTERACTION WITH COX11.
RX PubMed=15840172; DOI=10.1186/1744-8069-1-15;
RA Guo D., Ling J., Wang M.-H., She J.-X., Gu J., Wang C.-Y.;
RT "Physical interaction and functional coupling between ACDP4 and the
RT intracellular ion chaperone COX11, an implication of the role of ACDP4 in
RT essential metal ion transport and homeostasis.";
RL Mol. Pain 1:15-15(2005).
RN [8]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=22399287; DOI=10.1074/jbc.m112.342204;
RA de Baaij J.H., Stuiver M., Meij I.C., Lainez S., Kopplin K., Venselaar H.,
RA Mueller D., Bindels R.J., Hoenderop J.G.;
RT "Membrane topology and intracellular processing of Cyclin M2 (CNNM2).";
RL J. Biol. Chem. 287:13644-13655(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660 AND SER-664, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-134.
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 [11]
RP VARIANTS JALIS PRO-196; TYR-200 AND PRO-324, AND FUNCTION.
RX PubMed=19200525; DOI=10.1016/j.ajhg.2009.01.009;
RA Parry D.A., Mighell A.J., El-Sayed W., Shore R.C., Jalili I.K., Dollfus H.,
RA Bloch-Zupan A., Carlos R., Carr I.M., Downey L.M., Blain K.M.,
RA Mansfield D.C., Shahrabi M., Heidari M., Aref P., Abbasi M.,
RA Michaelides M., Moore A.T., Kirkham J., Inglehearn C.F.;
RT "Mutations in CNNM4 cause Jalili syndrome, consisting of autosomal-
RT recessive cone-rod dystrophy and amelogenesis imperfecta.";
RL Am. J. Hum. Genet. 84:266-273(2009).
CC -!- FUNCTION: Probable metal transporter. The interaction with the metal
CC ion chaperone COX11 suggests that it may play a role in sensory neuron
CC functions (By similarity). May play a role in biomineralization and
CC retinal function. {ECO:0000250, ECO:0000269|PubMed:19200525,
CC ECO:0000269|PubMed:19200527}.
CC -!- SUBUNIT: Interacts with COX11. {ECO:0000269|PubMed:15840172}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22399287};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22399287}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P4Q7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P4Q7-2; Sequence=VSP_054271, VSP_054272;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart.
CC {ECO:0000269|PubMed:12657465}.
CC -!- DISEASE: Jalili syndrome (JALIS) [MIM:217080]: A syndrome characterized
CC by the association of cone-rod dystrophy and amelogenesis imperfecta.
CC {ECO:0000269|PubMed:19200525, ECO:0000269|PubMed:19200527}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin family,
CC explaining its name. However, it has no cyclin-like function in vivo.
CC -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86370.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAY14963.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14266.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK022833; BAB14266.1; ALT_INIT; mRNA.
DR EMBL; AK293915; BAH11626.1; -; mRNA.
DR EMBL; AC092636; AAY14963.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC063295; AAH63295.2; -; mRNA.
DR EMBL; FJ619522; ACV32670.1; -; Genomic_DNA.
DR EMBL; FJ619523; ACV32671.1; -; Genomic_DNA.
DR EMBL; FJ619524; ACV32672.1; -; Genomic_DNA.
DR EMBL; AF202777; AAF86370.1; ALT_FRAME; mRNA.
DR EMBL; AB046812; BAB13418.1; -; mRNA.
DR CCDS; CCDS2024.2; -. [Q6P4Q7-1]
DR RefSeq; NP_064569.3; NM_020184.3. [Q6P4Q7-1]
DR PDB; 6G52; X-ray; 3.69 A; A/B/C/D/E/F/G/H/I=545-730.
DR PDB; 6RS2; X-ray; 3.69 A; A/B/C/D=359-511.
DR PDBsum; 6G52; -.
DR PDBsum; 6RS2; -.
DR AlphaFoldDB; Q6P4Q7; -.
DR SASBDB; Q6P4Q7; -.
DR SMR; Q6P4Q7; -.
DR BioGRID; 117711; 99.
DR IntAct; Q6P4Q7; 11.
DR MINT; Q6P4Q7; -.
DR STRING; 9606.ENSP00000366275; -.
DR TCDB; 1.A.112.1.4; the cyclin m mg2+ exporter (cnnm) family.
DR GlyConnect; 1504; 6 N-Linked glycans (2 sites).
DR GlyGen; Q6P4Q7; 4 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q6P4Q7; -.
DR PhosphoSitePlus; Q6P4Q7; -.
DR BioMuta; CNNM4; -.
DR DMDM; 224471892; -.
DR EPD; Q6P4Q7; -.
DR jPOST; Q6P4Q7; -.
DR MassIVE; Q6P4Q7; -.
DR MaxQB; Q6P4Q7; -.
DR PaxDb; Q6P4Q7; -.
DR PeptideAtlas; Q6P4Q7; -.
DR PRIDE; Q6P4Q7; -.
DR ProteomicsDB; 6371; -.
DR ProteomicsDB; 66982; -. [Q6P4Q7-1]
DR Antibodypedia; 17482; 156 antibodies from 21 providers.
DR DNASU; 26504; -.
DR Ensembl; ENST00000377075.3; ENSP00000366275.2; ENSG00000158158.12. [Q6P4Q7-1]
DR GeneID; 26504; -.
DR KEGG; hsa:26504; -.
DR MANE-Select; ENST00000377075.3; ENSP00000366275.2; NM_020184.4; NP_064569.3.
DR UCSC; uc002swx.3; human. [Q6P4Q7-1]
DR CTD; 26504; -.
DR DisGeNET; 26504; -.
DR GeneCards; CNNM4; -.
DR HGNC; HGNC:105; CNNM4.
DR HPA; ENSG00000158158; Tissue enhanced (retina).
DR MalaCards; CNNM4; -.
DR MIM; 217080; phenotype.
DR MIM; 607805; gene.
DR neXtProt; NX_Q6P4Q7; -.
DR OpenTargets; ENSG00000158158; -.
DR Orphanet; 1873; Jalili syndrome.
DR PharmGKB; PA26671; -.
DR VEuPathDB; HostDB:ENSG00000158158; -.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000156317; -.
DR HOGENOM; CLU_011310_1_1_1; -.
DR InParanoid; Q6P4Q7; -.
DR OMA; KLMFMHA; -.
DR OrthoDB; 1446644at2759; -.
DR PhylomeDB; Q6P4Q7; -.
DR TreeFam; TF101012; -.
DR BRENDA; 7.2.2.14; 2681.
DR PathwayCommons; Q6P4Q7; -.
DR SignaLink; Q6P4Q7; -.
DR BioGRID-ORCS; 26504; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; CNNM4; human.
DR GenomeRNAi; 26504; -.
DR Pharos; Q6P4Q7; Tbio.
DR PRO; PR:Q6P4Q7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6P4Q7; protein.
DR Bgee; ENSG00000158158; Expressed in mucosa of transverse colon and 113 other tissues.
DR Genevisible; Q6P4Q7; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
DR GO; GO:0010960; P:magnesium ion homeostasis; IBA:GO_Central.
DR GO; GO:0015693; P:magnesium ion transport; IBA:GO_Central.
DR GO; GO:0055065; P:metal ion homeostasis; IDA:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR045095; ACDP.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR12064; PTHR12064; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01595; DUF21; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51846; CNNM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amelogenesis imperfecta;
KW Biomineralization; CBS domain; Cell membrane; Cone-rod dystrophy;
KW Disease variant; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision.
FT CHAIN 1..775
FT /note="Metal transporter CNNM4"
FT /id="PRO_0000295765"
FT TOPO_DOM 1..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 178..358
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 377..438
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 445..511
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZF7"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..513
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054271"
FT VAR_SEQ 711..775
FT /note="ITRQQYQNGLLASRMENSPQFPIDGCTTHMENLAEKSELPVVDETTTLLNER
FT NSLLHKASHENAI -> PQSWPCFSRPGDRVCLPAPPSMNSSLPHADHSAAVPERAAGF
FT SHGEQPSVSHRRVHHPHGELGREV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054272"
FT VARIANT 126
FT /note="G -> R (in dbSNP:rs17855817)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033365"
FT VARIANT 134
FT /note="V -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035946"
FT VARIANT 196
FT /note="S -> P (in JALIS)"
FT /evidence="ECO:0000269|PubMed:19200525"
FT /id="VAR_058319"
FT VARIANT 200
FT /note="S -> Y (in JALIS; dbSNP:rs79424354)"
FT /evidence="ECO:0000269|PubMed:19200525"
FT /id="VAR_058320"
FT VARIANT 236
FT /note="R -> Q (in JALIS; dbSNP:rs75267011)"
FT /evidence="ECO:0000269|PubMed:19200527"
FT /id="VAR_058321"
FT VARIANT 324
FT /note="L -> P (in JALIS; dbSNP:rs74552543)"
FT /evidence="ECO:0000269|PubMed:19200525,
FT ECO:0000269|PubMed:19200527"
FT /id="VAR_058322"
FT CONFLICT 302
FT /note="T -> I (in Ref. 5; AAF86370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 86607 MW; D159303834A9416C CRC64;
MAPVGGGGRP VGGPARGRLL LAAPVLLVLL WALGARGQGS PQQGTIVGMR LASCNKSCGT
NPDGIIFVSE GSTVNLRLYG YSLGNISSNL ISFTEVDDAE TLHKSTSCLE LTKDLVVQQL
VNVSRGNTSG VLVVLTKFLR RSESMKLYAL CTRAQPDGPW LKWTDKDSLL FMVEEPGRFL
PLWLHILLIT VLLVLSGIFS GLNLGLMALD PMELRIVQNC GTEKERRYAR KIEPIRRKGN
YLLCSLLLGN VLVNTSLTIL LDNLIGSGLM AVASSTIGIV IFGEILPQAL CSRHGLAVGA
NTILLTKFFM LLTFPLSFPI SKLLDFFLGQ EIRTVYNREK LMEMLKVTEP YNDLVKEELN
MIQGALELRT KTVEDIMTQL QDCFMIRSDA ILDFNTMSEI MESGYTRIPV FEDEQSNIVD
ILYVKDLAFV DPDDCTPLKT ITRFYNHPVH FVFHDTKLDA MLEEFKKGKS HLAIVQKVNN
EGEGDPFYEV LGLVTLEDVI EEIIKSEILD ESDMYTDNRS RKRVSEKNKR DFSAFKDADN
ELKVKISPQL LLAAHRFLAT EVSQFSPSLI SEKILLRLLK YPDVIQELKF DEHNKYYARH
YLYTRNKPAD YFILILQGKV EVEAGKENMK FETGAFSYYG TMALTSVPSD RSPAHPTPLS
RSASLSYPDR TDVSTAATLA GSSNQFGSSV LGQYISDFSV RALVDLQYIK ITRQQYQNGL
LASRMENSPQ FPIDGCTTHM ENLAEKSELP VVDETTTLLN ERNSLLHKAS HENAI
