ACSF2_HUMAN
ID ACSF2_HUMAN Reviewed; 615 AA.
AC Q96CM8; B4DFQ6; B4DHT5; B4DUF5; Q9H7G2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Medium-chain acyl-CoA ligase ACSF2, mitochondrial {ECO:0000305};
DE EC=6.2.1.2 {ECO:0000269|PubMed:17762044};
DE Flags: Precursor;
GN Name=ACSF2 {ECO:0000312|HGNC:HGNC:26101}; ORFNames=UNQ493/PRO1009;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Adipose tissue, Amygdala, and Caudate nucleus;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-75.
RC TISSUE=Kidney, and Skin;
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 FUNCTION, AND INDUCTION.
RX PubMed=16380219; DOI=10.1016/j.gene.2005.10.021;
RA Perera R.J., Marcusson E.G., Koo S., Kang X., Kim Y., White N., Dean N.M.;
RT "Identification of novel PPARgamma target genes in primary human
RT adipocytes.";
RL Gene 369:90-99(2006).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17762044; DOI=10.1194/jlr.m700378-jlr200;
RA Watkins P.A., Maiguel D., Jia Z., Pevsner J.;
RT "Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human
RT genome.";
RL J. Lipid Res. 48:2736-2750(2007).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Acyl-CoA synthases catalyze the initial reaction in fatty
CC acid metabolism, by forming a thioester with CoA (PubMed:17762044). Has
CC some preference toward medium-chain substrates (PubMed:17762044). Plays
CC a role in adipocyte differentiation (PubMed:16380219).
CC {ECO:0000269|PubMed:16380219, ECO:0000269|PubMed:17762044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000269|PubMed:17762044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:17762044};
CC -!- INTERACTION:
CC Q96CM8; Q6RW13: AGTRAP; NbExp=4; IntAct=EBI-2876502, EBI-741181;
CC Q96CM8; Q6Q788: APOA5; NbExp=3; IntAct=EBI-2876502, EBI-3936819;
CC Q96CM8; P02654: APOC1; NbExp=3; IntAct=EBI-2876502, EBI-1220105;
CC Q96CM8; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2876502, EBI-11343438;
CC Q96CM8; Q15041: ARL6IP1; NbExp=8; IntAct=EBI-2876502, EBI-714543;
CC Q96CM8; Q8IYJ2-2: C10orf67; NbExp=3; IntAct=EBI-2876502, EBI-13381098;
CC Q96CM8; Q8IUN9: CLEC10A; NbExp=3; IntAct=EBI-2876502, EBI-2873246;
CC Q96CM8; Q96DZ9: CMTM5; NbExp=5; IntAct=EBI-2876502, EBI-2548702;
CC Q96CM8; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2876502, EBI-11522780;
CC Q96CM8; O75208: COQ9; NbExp=4; IntAct=EBI-2876502, EBI-724524;
CC Q96CM8; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-2876502, EBI-12831978;
CC Q96CM8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2876502, EBI-13345167;
CC Q96CM8; Q5XKP0: MICOS13; NbExp=3; IntAct=EBI-2876502, EBI-1053887;
CC Q96CM8; Q8IZV5: RDH10; NbExp=3; IntAct=EBI-2876502, EBI-11913715;
CC Q96CM8; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-2876502, EBI-17589229;
CC Q96CM8; Q9HC62: SENP2; NbExp=3; IntAct=EBI-2876502, EBI-714881;
CC Q96CM8; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2876502, EBI-2623095;
CC Q96CM8; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-2876502, EBI-17640454;
CC Q96CM8; O43761: SYNGR3; NbExp=3; IntAct=EBI-2876502, EBI-11321949;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96CM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96CM8-2; Sequence=VSP_055804;
CC Name=3;
CC IsoId=Q96CM8-3; Sequence=VSP_055805;
CC Name=4;
CC IsoId=Q96CM8-4; Sequence=VSP_055803;
CC -!- INDUCTION: By PPARG. {ECO:0000269|PubMed:16380219}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY358660; AAQ89023.1; -; mRNA.
DR EMBL; AK024573; BAB14930.1; -; mRNA.
DR EMBL; AK294205; BAG57517.1; -; mRNA.
DR EMBL; AK295258; BAG58247.1; -; mRNA.
DR EMBL; AK300625; BAG62317.1; -; mRNA.
DR EMBL; AC004707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC021491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94612.1; -; Genomic_DNA.
DR EMBL; BC012053; AAH12053.1; -; mRNA.
DR EMBL; BC014123; AAH14123.1; -; mRNA.
DR CCDS; CCDS11567.1; -. [Q96CM8-1]
DR CCDS; CCDS74103.1; -. [Q96CM8-2]
DR CCDS; CCDS74104.1; -. [Q96CM8-3]
DR RefSeq; NP_001275897.1; NM_001288968.1. [Q96CM8-2]
DR RefSeq; NP_001275898.1; NM_001288969.1. [Q96CM8-3]
DR RefSeq; NP_001275899.1; NM_001288970.1.
DR RefSeq; NP_001275900.1; NM_001288971.1. [Q96CM8-4]
DR RefSeq; NP_001275901.1; NM_001288972.1. [Q96CM8-4]
DR RefSeq; NP_079425.3; NM_025149.5. [Q96CM8-1]
DR AlphaFoldDB; Q96CM8; -.
DR SMR; Q96CM8; -.
DR BioGRID; 123187; 130.
DR IntAct; Q96CM8; 34.
DR MINT; Q96CM8; -.
DR STRING; 9606.ENSP00000401831; -.
DR SwissLipids; SLP:000001145; -.
DR GlyGen; Q96CM8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96CM8; -.
DR PhosphoSitePlus; Q96CM8; -.
DR BioMuta; ACSF2; -.
DR DMDM; 166198367; -.
DR CPTAC; CPTAC-5; -.
DR CPTAC; CPTAC-6; -.
DR EPD; Q96CM8; -.
DR jPOST; Q96CM8; -.
DR MassIVE; Q96CM8; -.
DR MaxQB; Q96CM8; -.
DR PaxDb; Q96CM8; -.
DR PeptideAtlas; Q96CM8; -.
DR PRIDE; Q96CM8; -.
DR ProteomicsDB; 4067; -.
DR ProteomicsDB; 4247; -.
DR ProteomicsDB; 5184; -.
DR ProteomicsDB; 76194; -. [Q96CM8-1]
DR TopDownProteomics; Q96CM8-1; -. [Q96CM8-1]
DR Antibodypedia; 30532; 140 antibodies from 24 providers.
DR DNASU; 80221; -.
DR Ensembl; ENST00000300441.9; ENSP00000300441.4; ENSG00000167107.13. [Q96CM8-1]
DR Ensembl; ENST00000427954.6; ENSP00000401831.2; ENSG00000167107.13. [Q96CM8-2]
DR Ensembl; ENST00000502667.5; ENSP00000421884.1; ENSG00000167107.13. [Q96CM8-3]
DR GeneID; 80221; -.
DR KEGG; hsa:80221; -.
DR MANE-Select; ENST00000300441.9; ENSP00000300441.4; NM_025149.6; NP_079425.3.
DR UCSC; uc002iqu.4; human. [Q96CM8-1]
DR CTD; 80221; -.
DR DisGeNET; 80221; -.
DR GeneCards; ACSF2; -.
DR HGNC; HGNC:26101; ACSF2.
DR HPA; ENSG00000167107; Tissue enhanced (kidney).
DR MIM; 610465; gene.
DR neXtProt; NX_Q96CM8; -.
DR OpenTargets; ENSG00000167107; -.
DR PharmGKB; PA162375338; -.
DR VEuPathDB; HostDB:ENSG00000167107; -.
DR eggNOG; KOG1177; Eukaryota.
DR GeneTree; ENSGT00940000156830; -.
DR HOGENOM; CLU_000022_59_7_1; -.
DR InParanoid; Q96CM8; -.
DR OMA; KQSDMKA; -.
DR OrthoDB; 386992at2759; -.
DR PhylomeDB; Q96CM8; -.
DR TreeFam; TF313466; -.
DR PathwayCommons; Q96CM8; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; Q96CM8; -.
DR BioGRID-ORCS; 80221; 18 hits in 1079 CRISPR screens.
DR ChiTaRS; ACSF2; human.
DR GenomeRNAi; 80221; -.
DR Pharos; Q96CM8; Tbio.
DR PRO; PR:Q96CM8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96CM8; protein.
DR Bgee; ENSG00000167107; Expressed in right lobe of thyroid gland and 153 other tissues.
DR ExpressionAtlas; Q96CM8; baseline and differential.
DR Genevisible; Q96CM8; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; TAS:Reactome.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; TAS:Reactome.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Fatty acid metabolism;
KW Ligase; Lipid metabolism; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..615
FT /note="Medium-chain acyl-CoA ligase ACSF2, mitochondrial"
FT /id="PRO_0000315793"
FT BINDING 263..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 182
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 182
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 340
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 398
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 478
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 510
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 544
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 544
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 570
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 570
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT MOD_RES 599
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCW8"
FT VAR_SEQ 1..160
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055803"
FT VAR_SEQ 43
FT /note="S -> SARGGMEAGRQRISVPSSFTASAAAH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055804"
FT VAR_SEQ 146..158
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055805"
FT VARIANT 75
FT /note="G -> V (in dbSNP:rs17856448)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038304"
FT VARIANT 316
FT /note="V -> M (in dbSNP:rs3744523)"
FT /id="VAR_038305"
SQ SEQUENCE 615 AA; 68125 MW; A3356EEA7C14730B CRC64;
MAVYVGMLRL GRLCAGSSGV LGARAALSRS WQEARLQGVR FLSSREVDRM VSTPIGGLSY
VQGCTKKHLN SKTVGQCLET TAQRVPEREA LVVLHEDVRL TFAQLKEEVD KAASGLLSIG
LCKGDRLGMW GPNSYAWVLM QLATAQAGII LVSVNPAYQA MELEYVLKKV GCKALVFPKQ
FKTQQYYNVL KQICPEVENA QPGALKSQRL PDLTTVISVD APLPGTLLLD EVVAAGSTRQ
HLDQLQYNQQ FLSCHDPINI QFTSGTTGSP KGATLSHYNI VNNSNILGER LKLHEKTPEQ
LRMILPNPLY HCLGSVAGTM MCLMYGATLI LASPIFNGKK ALEAISRERG TFLYGTPTMF
VDILNQPDFS SYDISTMCGG VIAGSPAPPE LIRAIINKIN MKDLVVAYGT TENSPVTFAH
FPEDTVEQKA ESVGRIMPHT EARIMNMEAG TLAKLNTPGE LCIRGYCVML GYWGEPQKTE
EAVDQDKWYW TGDVATMNEQ GFCKIVGRSK DMIIRGGENI YPAELEDFFH THPKVQEVQV
VGVKDDRMGE EICACIRLKD GEETTVEEIK AFCKGKISHF KIPKYIVFVT NYPLTISGKI
QKFKLREQME RHLNL
