S10AB_HUMAN
ID S10AB_HUMAN Reviewed; 105 AA.
AC P31949; Q5VTK0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Protein S100-A11;
DE AltName: Full=Calgizzarin;
DE AltName: Full=Metastatic lymph node gene 70 protein;
DE Short=MLN 70;
DE AltName: Full=Protein S100-C;
DE AltName: Full=S100 calcium-binding protein A11;
DE Contains:
DE RecName: Full=Protein S100-A11, N-terminally processed;
GN Name=S100A11; Synonyms=MLN70, S100C;
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].
RX PubMed=7889529; DOI=10.1016/0304-3835(94)03687-e;
RA Tanaka M., Adzuma K., Iwami M., Yoshimoto K., Monden Y., Itakura M.;
RT "Human calgizzarin; one colorectal cancer-related gene selected by a large
RT scale random cDNA sequencing and northern blot analysis.";
RL Cancer Lett. 89:195-200(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=7490069; DOI=10.1006/geno.1995.1163;
RA Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P.,
RA Lidereau R., Basset P., Rio M.-C.;
RT "Identification of four novel human genes amplified and overexpressed in
RT breast carcinoma and localized to the q11-q21.3 region of chromosome 17.";
RL Genomics 28:367-376(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Nakatani K., Kato A., Sugimoto M., Kumano K., Komada T., Tsunoda H.,
RA Ito M., Nakano T., Shima T., Tanaka T.;
RT "Isolation and characterization of cDNA for human S100C protein and a
RT related gene.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S.,
RA Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M.,
RA Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y.;
RT "Molecular cloning of a human homologue of the two calcium binding protein,
RT porcine S100 and rabbit calgizzarin.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Urinary bladder;
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 PROTEIN SEQUENCE OF 4-12; 43-51 AND 56-62.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-6, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP 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 [16]
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).
RN [17]
RP STRUCTURE BY NMR OF 1-19, DISULFIDE BOND, PHOSPHORYLATION AT THR-10,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18618420; DOI=10.1002/psc.1050;
RA Kouno T., Mizuguchi M., Sakaguchi M., Makino E., Mori Y., Shinoda H.,
RA Aizawa T., Demura M., Huh N.H., Kawano K.;
RT "The structure of S100A11 fragment explains a local structural change
RT induced by phosphorylation.";
RL J. Pept. Sci. 14:1129-1138(2008).
CC -!- FUNCTION: Facilitates the differentiation and the cornification of
CC keratinocytes. {ECO:0000269|PubMed:18618420}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:18618420}.
CC -!- INTERACTION:
CC P31949; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-701862, EBI-741158;
CC P31949; P04271: S100B; NbExp=5; IntAct=EBI-701862, EBI-458391;
CC P31949; P04637: TP53; NbExp=2; IntAct=EBI-701862, EBI-366083;
CC P31949; Q8TD43: TRPM4; NbExp=2; IntAct=EBI-701862, EBI-11723041;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18618420}. Nucleus
CC {ECO:0000269|PubMed:18618420}.
CC -!- PTM: Phosphorylation at Thr-10 by PRKCA significantly suppresses
CC homodimerization and promotes association with NCL/nucleolin which
CC induces nuclear translocation. {ECO:0000269|PubMed:18618420}.
CC -!- MISCELLANEOUS: Binds two calcium ions per molecule with an affinity
CC similar to that of the S-100 proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; D38583; BAA07597.1; -; mRNA.
DR EMBL; X80201; CAA56492.1; -; mRNA.
DR EMBL; D49355; BAA08354.1; -; mRNA.
DR EMBL; D50374; BAA23325.1; -; mRNA.
DR EMBL; BT009912; AAP88914.1; -; mRNA.
DR EMBL; AL591893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001410; AAH01410.1; -; mRNA.
DR EMBL; BC014354; AAH14354.1; -; mRNA.
DR CCDS; CCDS1009.1; -.
DR PIR; I37080; I37080.
DR RefSeq; NP_005611.1; NM_005620.1.
DR PDB; 1V4Z; NMR; -; A=1-19.
DR PDB; 1V50; NMR; -; A=1-19.
DR PDB; 2LUC; NMR; -; A/B=1-105.
DR PDBsum; 1V4Z; -.
DR PDBsum; 1V50; -.
DR PDBsum; 2LUC; -.
DR AlphaFoldDB; P31949; -.
DR BMRB; P31949; -.
DR SMR; P31949; -.
DR BioGRID; 112190; 42.
DR IntAct; P31949; 22.
DR MINT; P31949; -.
DR STRING; 9606.ENSP00000271638; -.
DR DrugBank; DB02482; Phosphonothreonine.
DR GlyGen; P31949; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P31949; -.
DR MetOSite; P31949; -.
DR PhosphoSitePlus; P31949; -.
DR SwissPalm; P31949; -.
DR BioMuta; S100A11; -.
DR DMDM; 1710818; -.
DR DOSAC-COBS-2DPAGE; P31949; -.
DR SWISS-2DPAGE; P31949; -.
DR EPD; P31949; -.
DR jPOST; P31949; -.
DR MassIVE; P31949; -.
DR PaxDb; P31949; -.
DR PeptideAtlas; P31949; -.
DR PRIDE; P31949; -.
DR ProteomicsDB; 54821; -.
DR TopDownProteomics; P31949; -.
DR Antibodypedia; 20339; 455 antibodies from 35 providers.
DR DNASU; 6282; -.
DR Ensembl; ENST00000271638.3; ENSP00000271638.2; ENSG00000163191.6.
DR GeneID; 6282; -.
DR KEGG; hsa:6282; -.
DR MANE-Select; ENST00000271638.3; ENSP00000271638.2; NM_005620.2; NP_005611.1.
DR CTD; 6282; -.
DR DisGeNET; 6282; -.
DR GeneCards; S100A11; -.
DR HGNC; HGNC:10488; S100A11.
DR HPA; ENSG00000163191; Tissue enhanced (esophagus).
DR MIM; 603114; gene.
DR neXtProt; NX_P31949; -.
DR OpenTargets; ENSG00000163191; -.
DR PharmGKB; PA34900; -.
DR VEuPathDB; HostDB:ENSG00000163191; -.
DR eggNOG; ENOG502SS6H; Eukaryota.
DR GeneTree; ENSGT00940000154172; -.
DR HOGENOM; CLU_138624_1_0_1; -.
DR InParanoid; P31949; -.
DR OMA; MACEKCY; -.
DR OrthoDB; 1549220at2759; -.
DR PhylomeDB; P31949; -.
DR TreeFam; TF332727; -.
DR PathwayCommons; P31949; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P31949; -.
DR BioGRID-ORCS; 6282; 23 hits in 1041 CRISPR screens.
DR ChiTaRS; S100A11; human.
DR EvolutionaryTrace; P31949; -.
DR GeneWiki; S100A11; -.
DR GenomeRNAi; 6282; -.
DR Pharos; P31949; Tbio.
DR PRO; PR:P31949; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P31949; protein.
DR Bgee; ENSG00000163191; Expressed in lower esophagus mucosa and 206 other tissues.
DR ExpressionAtlas; P31949; baseline and differential.
DR Genevisible; P31949; HS.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0008156; P:negative regulation of DNA replication; TAS:ProtInc.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:CACAO.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028482; S100A11.
DR PANTHER; PTHR11639:SF60; PTHR11639:SF60; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..105
FT /note="Protein S100-A11"
FT /id="PRO_0000424465"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..105
FT /note="Protein S100-A11, N-terminally processed"
FT /id="PRO_0000144009"
FT DOMAIN 13..49
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 55..90
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylalanine; in Protein S100-A11, N-terminally
FT processed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18618420"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50543"
FT DISULFID 13
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18618420"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:1V4Z"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2LUC"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:2LUC"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:2LUC"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:2LUC"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2LUC"
FT HELIX 77..96
FT /evidence="ECO:0007829|PDB:2LUC"
SQ SEQUENCE 105 AA; 11740 MW; 1729ED680290CFE4 CRC64;
MAKISSPTET ERCIESLIAV FQKYAGKDGY NYTLSKTEFL SFMNTELAAF TKNQKDPGVL
DRMMKKLDTN SDGQLDFSEF LNLIGGLAMA CHDSFLKAVP SQKRT
