SCD5_HUMAN
ID SCD5_HUMAN Reviewed; 330 AA.
AC Q86SK9; B2RPG0; Q4W5Q5; Q8NDS0; Q9H7D1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Stearoyl-CoA desaturase 5 {ECO:0000303|PubMed:22745828};
DE EC=1.14.19.1 {ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:22745828};
DE AltName: Full=Acyl-CoA-desaturase 4 {ECO:0000303|PubMed:12727354};
DE AltName: Full=HSCD5 {ECO:0000303|PubMed:15907797};
DE AltName: Full=Stearoyl-CoA 9-desaturase {ECO:0000303|PubMed:15907797};
DE AltName: Full=Stearoyl-CoA desaturase 2 {ECO:0000303|PubMed:15610069};
GN Name=SCD5;
GN Synonyms=ACOD4 {ECO:0000303|PubMed:12727354},
GN SCD2 {ECO:0000303|PubMed:15610069}, SCD4;
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 TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12727354; DOI=10.1016/s0378-1119(03)00461-x;
RA Beiraghi S., Zhou M., Talmadge C.B., Went-Sumegi N., Davis J.R., Huang D.,
RA Saal H., Seemayer T.A., Sumegi J.;
RT "Identification and characterization of a novel gene disrupted by a
RT pericentric inversion inv(4)(p13.1q21.1) in a family with cleft lip.";
RL Gene 309:11-21(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endothelial cell;
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=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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-330.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15907797; DOI=10.1016/j.bbrc.2005.05.013;
RA Wang J., Yu L., Schmidt R.E., Su C., Huang X., Gould K., Cao G.;
RT "Characterization of HSCD5, a novel human stearoyl-CoA desaturase unique to
RT primates.";
RL Biochem. Biophys. Res. Commun. 332:735-742(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBUNIT.
RX PubMed=15610069; DOI=10.1042/bj20041554;
RA Zhang S., Yang Y., Shi Y.;
RT "Characterization of human SCD2, an oligomeric desaturase with improved
RT stability and enzyme activity by cross-linking in intact cells.";
RL Biochem. J. 388:135-142(2005).
RN [9]
RP CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22745828; DOI=10.1371/journal.pone.0039787;
RA Sinner D.I., Kim G.J., Henderson G.C., Igal R.A.;
RT "StearoylCoA desaturase-5: a novel regulator of neuronal cell proliferation
RT and differentiation.";
RL PLoS ONE 7:e39787-e39787(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP TISSUE SPECIFICITY, INVOLVEMENT IN DFNA79, AND VARIANT DFNA79 SER-209.
RX PubMed=31972369; DOI=10.1016/j.ejmg.2020.103855;
RA Lu X., Zhang Y., Chen L., Wang Q., Zeng Z., Dong C., Qi Y., Liu Y.;
RT "Whole exome sequencing identifies SCD5 as a novel causative gene for
RT autosomal dominant nonsyndromic deafness.";
RL Eur. J. Med. Genet. 63:103855-103855(2020).
CC -!- FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC reduced cytochrome b5 to introduce the first double bond into saturated
CC fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond
CC at the delta-9 position into fatty acyl-CoA substrates including
CC palmitoyl-CoA and stearoyl-CoA (PubMed:15610069, PubMed:15907797,
CC PubMed:22745828). Gives rise to a mixture of 16:1 and 18:1 unsaturated
CC fatty acids (PubMed:15610069, PubMed:15907797). Involved in neuronal
CC cell proliferation and differentiation through down-regulation of
CC EGFR/AKT/MAPK and Wnt signaling pathways (PubMed:22745828).
CC {ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797,
CC ECO:0000269|PubMed:22745828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36931, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:15610069,
CC ECO:0000269|PubMed:22745828};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P13516};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:P13516};
CC -!- SUBUNIT: May self-associate and form homodimers.
CC {ECO:0000269|PubMed:15610069}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15907797, ECO:0000269|PubMed:22745828}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86SK9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86SK9-2; Sequence=VSP_029883;
CC -!- TISSUE SPECIFICITY: Detected in fetal brain, and at lower levels in
CC fetal kidney. Detected in adult brain and pancreas, and at lower levels
CC in kidney and lung. Expressed in spiral ganglion cells and the organ of
CC Corti of fetal cochlea (PubMed:31972369). {ECO:0000269|PubMed:12727354,
CC ECO:0000269|PubMed:15610069, ECO:0000269|PubMed:15907797,
CC ECO:0000269|PubMed:22745828, ECO:0000269|PubMed:31972369}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- DISEASE: Deafness, autosomal dominant, 79 (DFNA79) [MIM:619086]: A form
CC of non-syndromic, progressive sensorineural hearing loss. Sensorineural
CC hearing loss results from damage to the neural receptors of the inner
CC ear, the nerve pathways to the brain, or the area of the brain that
CC receives sound information. DFNA79 affected females appear to have
CC milder hearing loss than males. {ECO:0000269|PubMed:31972369}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- MISCELLANEOUS: This protein has no ortholog in rodents. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF389338; AAP31443.1; -; mRNA.
DR EMBL; AK024685; BAB14961.1; -; mRNA.
DR EMBL; AC073413; AAY40977.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05903.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05904.1; -; Genomic_DNA.
DR EMBL; BC137429; AAI37430.1; -; mRNA.
DR EMBL; BC137432; AAI37433.1; -; mRNA.
DR EMBL; AL831891; CAD38567.1; -; mRNA.
DR CCDS; CCDS34024.1; -. [Q86SK9-1]
DR CCDS; CCDS3595.1; -. [Q86SK9-2]
DR RefSeq; NP_001032671.2; NM_001037582.2. [Q86SK9-1]
DR RefSeq; NP_079182.2; NM_024906.2. [Q86SK9-2]
DR AlphaFoldDB; Q86SK9; -.
DR SMR; Q86SK9; -.
DR BioGRID; 123034; 56.
DR IntAct; Q86SK9; 3.
DR STRING; 9606.ENSP00000316329; -.
DR BindingDB; Q86SK9; -.
DR ChEMBL; CHEMBL1275210; -.
DR SwissLipids; SLP:000001074; -.
DR iPTMnet; Q86SK9; -.
DR PhosphoSitePlus; Q86SK9; -.
DR BioMuta; SCD5; -.
DR DMDM; 162416247; -.
DR EPD; Q86SK9; -.
DR jPOST; Q86SK9; -.
DR MassIVE; Q86SK9; -.
DR MaxQB; Q86SK9; -.
DR PaxDb; Q86SK9; -.
DR PeptideAtlas; Q86SK9; -.
DR PRIDE; Q86SK9; -.
DR ProteomicsDB; 69599; -. [Q86SK9-1]
DR ProteomicsDB; 69600; -. [Q86SK9-2]
DR Antibodypedia; 51995; 100 antibodies from 17 providers.
DR DNASU; 79966; -.
DR Ensembl; ENST00000273908.4; ENSP00000273908.4; ENSG00000145284.12. [Q86SK9-2]
DR Ensembl; ENST00000319540.9; ENSP00000316329.4; ENSG00000145284.12. [Q86SK9-1]
DR GeneID; 79966; -.
DR KEGG; hsa:79966; -.
DR MANE-Select; ENST00000319540.9; ENSP00000316329.4; NM_001037582.3; NP_001032671.2.
DR UCSC; uc003hna.3; human. [Q86SK9-1]
DR CTD; 79966; -.
DR DisGeNET; 79966; -.
DR GeneCards; SCD5; -.
DR HGNC; HGNC:21088; SCD5.
DR HPA; ENSG00000145284; Tissue enhanced (adrenal gland, brain).
DR MalaCards; SCD5; -.
DR MIM; 608370; gene.
DR MIM; 619086; phenotype.
DR neXtProt; NX_Q86SK9; -.
DR OpenTargets; ENSG00000145284; -.
DR PharmGKB; PA134934692; -.
DR VEuPathDB; HostDB:ENSG00000145284; -.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00940000162090; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; Q86SK9; -.
DR OMA; CQHGPID; -.
DR PhylomeDB; Q86SK9; -.
DR TreeFam; TF313251; -.
DR BRENDA; 1.14.19.1; 2681.
DR PathwayCommons; Q86SK9; -.
DR Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; Q86SK9; -.
DR BioGRID-ORCS; 79966; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; SCD5; human.
DR GenomeRNAi; 79966; -.
DR Pharos; Q86SK9; Tchem.
DR PRO; PR:Q86SK9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q86SK9; protein.
DR Bgee; ENSG00000145284; Expressed in lateral globus pallidus and 193 other tissues.
DR Genevisible; Q86SK9; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:UniProtKB.
DR GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Deafness; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Non-syndromic deafness;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..330
FT /note="Stearoyl-CoA desaturase 5"
FT /id="PRO_0000312653"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..72
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 94..99
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 131..135
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 272..276
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 276
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT VAR_SEQ 190..330
FT /note="KYYKISVVLMCFVVPTLVPWYIWGESLWNSYFLASILRYTISLNISWLVNSA
FT AHMYGNRPYDKHISPRQNPLVALGAIGEGFHNYHHTFPFDYSASEFGLNFNPTTWFIDF
FT MCWLGLATDRKRATKPMIEARKARTGDSSA -> NTQHIQKEGRALNQEAACEMLREWH
FT QGHILKVTLPGLHILALLHTHCNHSEKCCLMLRALSVSLEVF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029883"
FT VARIANT 209
FT /note="W -> S (in DFNA79; unknown pathological
FT significance; dbSNP:rs192654796)"
FT /evidence="ECO:0000269|PubMed:31972369"
FT /id="VAR_085092"
FT CONFLICT 82
FT /note="F -> L (in Ref. 2; BAB14961)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="W -> R (in Ref. 1; AAP31443 and 2; BAB14961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 37610 MW; 50652E942C19DB82 CRC64;
MPGPATDAGK IPFCDAKEEI RAGLESSEGG GGPERPGARG QRQNIVWRNV VLMSLLHLGA
VYSLVLIPKA KPLTLLWAYF CFLLAALGVT AGAHRLWSHR SYRAKLPLRI FLAVANSMAF
QNDIFEWSRD HRAHHKYSET DADPHNARRG FFFSHIGWLF VRKHRDVIEK GRKLDVTDLL
ADPVVRIQRK YYKISVVLMC FVVPTLVPWY IWGESLWNSY FLASILRYTI SLNISWLVNS
AAHMYGNRPY DKHISPRQNP LVALGAIGEG FHNYHHTFPF DYSASEFGLN FNPTTWFIDF
MCWLGLATDR KRATKPMIEA RKARTGDSSA
