ALS_HUMAN
ID ALS_HUMAN Reviewed; 605 AA.
AC P35858; B4DZY8; E9PGU3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Insulin-like growth factor-binding protein complex acid labile subunit;
DE Short=ALS;
DE Flags: Precursor;
GN Name=IGFALS; Synonyms=ALS;
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), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1379671; DOI=10.1210/mend.6.6.1379671;
RA Leong S.R., Baxter R.C., Camerato T., Dai J., Wood W.I.;
RT "Structure and functional expression of the acid-labile subunit of the
RT insulin-like growth factor-binding protein complex.";
RL Mol. Endocrinol. 6:870-876(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10650966; DOI=10.1210/endo.141.2.7333;
RA Suwanichkul A., Boisclair Y.R., Olney R.C., Durham S.K., Powell D.R.;
RT "Conservation of a growth hormone-responsive promoter element in the human
RT and mouse acid-labile subunit genes.";
RL Endocrinology 141:833-838(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP PROTEIN SEQUENCE OF 28-35.
RX PubMed=2473065; DOI=10.1016/s0021-9258(18)80143-0;
RA Baxter R.C., Martin J.L., Beniac V.A.;
RT "High molecular weight insulin-like growth factor binding protein complex.
RT Purification and properties of the acid-labile subunit from human serum.";
RL J. Biol. Chem. 264:11843-11848(1989).
RN [6]
RP INVOLVEMENT IN ACLSD.
RX PubMed=14762184; DOI=10.1056/nejmoa013100;
RA Domene H.M., Bengolea S.V., Martinez A.S., Ropelato M.G., Pennisi P.,
RA Scaglia P., Heinrich J.J., Jasper H.G.;
RT "Deficiency of the circulating insulin-like growth factor system associated
RT with inactivation of the acid-labile subunit gene.";
RL N. Engl. J. Med. 350:570-577(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-368 AND ASN-515.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP VARIANT ACLSD ASN-440.
RX PubMed=16507628; DOI=10.1210/jc.2005-2842;
RA Hwa V., Haeusler G., Pratt K.L., Little B.M., Frisch H., Koller D.,
RA Rosenfeld R.G.;
RT "Total absence of functional acid labile subunit, resulting in severe
RT insulin-like growth factor deficiency and moderate growth failure.";
RL J. Clin. Endocrinol. Metab. 91:1826-1831(2006).
RN [9]
RP VARIANTS ACLSD SER-LEU-ARG-197 INS AND ARG-540.
RX PubMed=17726072; DOI=10.1210/jc.2007-1152;
RA Domene H.M., Scaglia P.A., Lteif A., Mahmud F.H., Kirmani S., Frystyk J.,
RA Bedecarras P., Gutierrez M., Jasper H.G.;
RT "Phenotypic effects of null and haploinsufficiency of acid-labile subunit
RT in a family with two novel IGFALS gene mutations.";
RL J. Clin. Endocrinol. Metab. 92:4444-4450(2007).
RN [10]
RP VARIANT ACLSD SER-276.
RX PubMed=18303074; DOI=10.1210/jc.2007-2678;
RA Heath K.E., Argente J., Barrios V., Pozo J., Diaz-Gonzalez F.,
RA Martos-Moreno G.A., Caimari M., Gracia R., Campos-Barros A.;
RT "Primary acid-labile subunit deficiency due to recessive IGFALS mutations
RT results in postnatal growth deficit associated with low circulating insulin
RT growth factor (IGF)-I, IGF binding protein-3 levels, and
RT hyperinsulinemia.";
RL J. Clin. Endocrinol. Metab. 93:1616-1624(2008).
RN [11]
RP VARIANTS ACLSD SER-60; PHE-244 AND LEU-GLU-LEU-439 INS.
RX PubMed=19129715; DOI=10.1159/000183899;
RA Fofanova-Gambetti O.V., Hwa V., Kirsch S., Pihoker C., Chiu H.K.,
RA Hogler W., Cohen L.E., Jacobsen C., Derr M.A., Rosenfeld R.G.;
RT "Three novel IGFALS gene mutations resulting in total ALS and severe
RT circulating IGF-I/IGFBP-3 deficiency in children of different ethnic
RT origins.";
RL Horm. Res. 71:100-110(2009).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-368.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP VARIANTS ACLSD LEU-73 AND GLN-134.
RX PubMed=20389102; DOI=10.1159/000308164;
RA David A., Rose S.J., Miraki-Moud F., Metherell L.A., Savage M.O.,
RA Clark A.J., Camacho-Huebner C.;
RT "Acid-labile subunit deficiency and growth failure: description of two
RT novel cases.";
RL Horm. Res. Paediatr. 73:328-334(2010).
RN [14]
RP INVOLVEMENT IN ACLSD.
RX PubMed=21396577; DOI=10.1016/j.beem.2010.08.010;
RA Domene H.M., Hwa V., Jasper H.G., Rosenfeld R.G.;
RT "Acid-labile subunit (ALS) deficiency.";
RL Best Pract. Res. Clin. Endocrinol. Metab. 25:101-113(2011).
RN [15]
RP VARIANT IN ACLSD PRO-127.
RX PubMed=23488611; DOI=10.1111/cen.12200;
RA Hess O., Khayat M., Hwa V., Heath K.E., Teitler A., Hritan Y.,
RA Allon-Shalev S., Tenenbaum-Rakover Y.;
RT "A novel mutation in IGFALS, c.380T>C (p.L127P), associated with short
RT stature, delayed puberty, osteopenia and hyperinsulinaemia in two siblings:
RT insights into the roles of insulin growth factor-1 (IGF1).";
RL Clin. Endocrinol. (Oxf.) 79:838-844(2013).
CC -!- FUNCTION: Involved in protein-protein interactions that result in
CC protein complexes, receptor-ligand binding or cell adhesion.
CC -!- SUBUNIT: Forms a ternary complex of about 140 to 150 kDa with IGF-I or
CC IGF-II and IGFBP-3.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35858-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35858-2; Sequence=VSP_044605;
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- DISEASE: Acid-labile subunit deficiency (ACLSD) [MIM:615961]: A
CC disorder characterized by severely reduced serum IGF-I and IGFBP-3
CC concentrations and mild growth retardation. Pubertal delay in boys and
CC insulin insensitivity are common findings.
CC {ECO:0000269|PubMed:14762184, ECO:0000269|PubMed:16507628,
CC ECO:0000269|PubMed:17726072, ECO:0000269|PubMed:18303074,
CC ECO:0000269|PubMed:19129715, ECO:0000269|PubMed:20389102,
CC ECO:0000269|PubMed:21396577, ECO:0000269|PubMed:23488611}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; M86826; AAA36047.1; -; mRNA.
DR EMBL; AF192554; AAF06774.1; -; Genomic_DNA.
DR EMBL; AK303146; BAG64250.1; -; mRNA.
DR EMBL; AC012180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031724; CAC36078.1; -; Genomic_DNA.
DR CCDS; CCDS10446.1; -. [P35858-1]
DR CCDS; CCDS53982.1; -. [P35858-2]
DR PIR; A41915; A41915.
DR RefSeq; NP_001139478.1; NM_001146006.1. [P35858-2]
DR RefSeq; NP_004961.1; NM_004970.2. [P35858-1]
DR AlphaFoldDB; P35858; -.
DR SMR; P35858; -.
DR BioGRID; 109704; 39.
DR CORUM; P35858; -.
DR STRING; 9606.ENSP00000416683; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01277; Mecasermin.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 1401; 7 N-Linked glycans (2 sites).
DR GlyGen; P35858; 7 sites, 7 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P35858; -.
DR PhosphoSitePlus; P35858; -.
DR BioMuta; IGFALS; -.
DR DMDM; 543800; -.
DR CPTAC; non-CPTAC-2678; -.
DR EPD; P35858; -.
DR jPOST; P35858; -.
DR MassIVE; P35858; -.
DR PaxDb; P35858; -.
DR PeptideAtlas; P35858; -.
DR PRIDE; P35858; -.
DR ProteomicsDB; 20394; -.
DR ProteomicsDB; 55158; -. [P35858-1]
DR Antibodypedia; 42497; 256 antibodies from 32 providers.
DR DNASU; 3483; -.
DR Ensembl; ENST00000215539.4; ENSP00000215539.3; ENSG00000099769.6. [P35858-1]
DR Ensembl; ENST00000415638.3; ENSP00000416683.3; ENSG00000099769.6. [P35858-2]
DR GeneID; 3483; -.
DR KEGG; hsa:3483; -.
DR MANE-Select; ENST00000215539.4; ENSP00000215539.3; NM_004970.3; NP_004961.1.
DR UCSC; uc002cmy.4; human. [P35858-1]
DR CTD; 3483; -.
DR DisGeNET; 3483; -.
DR GeneCards; IGFALS; -.
DR HGNC; HGNC:5468; IGFALS.
DR HPA; ENSG00000099769; Tissue enriched (liver).
DR MalaCards; IGFALS; -.
DR MIM; 601489; gene.
DR MIM; 615961; phenotype.
DR neXtProt; NX_P35858; -.
DR OpenTargets; ENSG00000099769; -.
DR Orphanet; 140941; Short stature due to primary acid-labile subunit deficiency.
DR PharmGKB; PA29702; -.
DR VEuPathDB; HostDB:ENSG00000099769; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160824; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; P35858; -.
DR OMA; WYLNLGW; -.
DR PhylomeDB; P35858; -.
DR TreeFam; TF351124; -.
DR PathwayCommons; P35858; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR SignaLink; P35858; -.
DR BioGRID-ORCS; 3483; 12 hits in 1068 CRISPR screens.
DR ChiTaRS; IGFALS; human.
DR GeneWiki; IGFALS; -.
DR GenomeRNAi; 3483; -.
DR Pharos; P35858; Tbio.
DR PRO; PR:P35858; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P35858; protein.
DR Bgee; ENSG00000099769; Expressed in right lobe of liver and 131 other tissues.
DR ExpressionAtlas; P35858; baseline and differential.
DR Genevisible; P35858; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042567; C:insulin-like growth factor ternary complex; IDA:BHF-UCL.
DR GO; GO:0005520; F:insulin-like growth factor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 5.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 19.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 18.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Direct protein sequencing;
KW Disease variant; Glycoprotein; Leucine-rich repeat; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:2473065"
FT CHAIN 28..605
FT /note="Insulin-like growth factor-binding protein complex
FT acid labile subunit"
FT /id="PRO_0000020695"
FT DOMAIN 32..74
FT /note="LRRNT"
FT REPEAT 75..96
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 123..144
FT /note="LRR 3"
FT REPEAT 147..168
FT /note="LRR 4"
FT REPEAT 171..192
FT /note="LRR 5"
FT REPEAT 195..216
FT /note="LRR 6"
FT REPEAT 219..240
FT /note="LRR 7"
FT REPEAT 243..264
FT /note="LRR 8"
FT REPEAT 267..288
FT /note="LRR 9"
FT REPEAT 291..312
FT /note="LRR 10"
FT REPEAT 315..336
FT /note="LRR 11"
FT REPEAT 339..360
FT /note="LRR 12"
FT REPEAT 363..384
FT /note="LRR 13"
FT REPEAT 387..408
FT /note="LRR 14"
FT REPEAT 411..432
FT /note="LRR 15"
FT REPEAT 435..456
FT /note="LRR 16"
FT REPEAT 459..480
FT /note="LRR 17"
FT REPEAT 483..504
FT /note="LRR 18"
FT REPEAT 507..528
FT /note="LRR 19"
FT DOMAIN 536..605
FT /note="LRRCT"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 5
FT /note="K -> KAGDLEPQFTPERRFRLCWYQAHSGRALLGPPPQASPPA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044605"
FT VARIANT 60
FT /note="C -> S (in ACLSD)"
FT /evidence="ECO:0000269|PubMed:19129715"
FT /id="VAR_072475"
FT VARIANT 73
FT /note="P -> L (in ACLSD; dbSNP:rs766004600)"
FT /evidence="ECO:0000269|PubMed:20389102"
FT /id="VAR_072476"
FT VARIANT 97
FT /note="L -> F (in dbSNP:rs35947557)"
FT /id="VAR_050658"
FT VARIANT 127
FT /note="L -> P (in ACLSD)"
FT /evidence="ECO:0000269|PubMed:23488611"
FT /id="VAR_074071"
FT VARIANT 134
FT /note="L -> Q (in ACLSD)"
FT /evidence="ECO:0000269|PubMed:20389102"
FT /id="VAR_072477"
FT VARIANT 197
FT /note="R -> RSLR (in ACLSD)"
FT /evidence="ECO:0000269|PubMed:17726072"
FT /id="VAR_072478"
FT VARIANT 244
FT /note="L -> F (in ACLSD; dbSNP:rs774634302)"
FT /evidence="ECO:0000269|PubMed:19129715"
FT /id="VAR_072479"
FT VARIANT 276
FT /note="N -> S (in ACLSD; dbSNP:rs551618643)"
FT /evidence="ECO:0000269|PubMed:18303074"
FT /id="VAR_072480"
FT VARIANT 307
FT /note="P -> L (in dbSNP:rs34297640)"
FT /id="VAR_050659"
FT VARIANT 439
FT /note="L -> LLEL (in ACLSD)"
FT /evidence="ECO:0000269|PubMed:19129715"
FT /id="VAR_072481"
FT VARIANT 440
FT /note="D -> N (in ACLSD; dbSNP:rs776840046)"
FT /evidence="ECO:0000269|PubMed:16507628"
FT /id="VAR_072482"
FT VARIANT 498
FT /note="P -> S (in dbSNP:rs9282730)"
FT /id="VAR_022034"
FT VARIANT 540
FT /note="C -> R (in ACLSD; dbSNP:rs121909247)"
FT /evidence="ECO:0000269|PubMed:17726072"
FT /id="VAR_072483"
FT VARIANT 548
FT /note="R -> W (in dbSNP:rs9282731)"
FT /id="VAR_022035"
FT CONFLICT 10
FT /note="L -> P (in Ref. 3; BAG64250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 66035 MW; F6562A23CBE918F6 CRC64;
MALRKGGLAL ALLLLSWVAL GPRSLEGADP GTPGEAEGPA CPAACVCSYD DDADELSVFC
SSRNLTRLPD GVPGGTQALW LDGNNLSSVP PAAFQNLSSL GFLNLQGGQL GSLEPQALLG
LENLCHLHLE RNQLRSLALG TFAHTPALAS LGLSNNRLSR LEDGLFEGLG SLWDLNLGWN
SLAVLPDAAF RGLGSLRELV LAGNRLAYLQ PALFSGLAEL RELDLSRNAL RAIKANVFVQ
LPRLQKLYLD RNLIAAVAPG AFLGLKALRW LDLSHNRVAG LLEDTFPGLL GLRVLRLSHN
AIASLRPRTF KDLHFLEELQ LGHNRIRQLA ERSFEGLGQL EVLTLDHNQL QEVKAGAFLG
LTNVAVMNLS GNCLRNLPEQ VFRGLGKLHS LHLEGSCLGR IRPHTFTGLS GLRRLFLKDN
GLVGIEEQSL WGLAELLELD LTSNQLTHLP HRLFQGLGKL EYLLLSRNRL AELPADALGP
LQRAFWLDVS HNRLEALPNS LLAPLGRLRY LSLRNNSLRT FTPQPPGLER LWLEGNPWDC
GCPLKALRDF ALQNPSAVPR FVQAICEGDD CQPPAYTYNN ITCASPPEVV GLDLRDLSEA
HFAPC
