ID   COPD_HUMAN              Reviewed;         511 AA.
AC   P48444; B4E1X2; E9PEU4; Q52M80;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Coatomer subunit delta;
DE   AltName: Full=Archain;
DE   AltName: Full=Delta-coat protein;
DE            Short=Delta-COP;
GN   Name=ARCN1; Synonyms=COPD;
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).
RX   PubMed=7782067; DOI=10.1016/0888-7543(95)80087-3;
RA   Radice P., Pensotti V., Jones C., Perry H., Pierotti M.A., Tunnacliffe A.;
RT   "The human archain gene, ARCN1, has highly conserved homologs in rice and
RT   Drosophila.";
RL   Genomics 26:101-106(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Trachea;
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=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
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   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-309, AND
RP   IDENTIFICATION BY MASS 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP   MASS 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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [9]
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; SER-244 AND SER-493, 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   [11]
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   [12]
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   [13]
RP   INVOLVEMENT IN SSMG.
RX   PubMed=27476655; DOI=10.1016/j.ajhg.2016.06.011;
RA   Izumi K., Brett M., Nishi E., Drunat S., Tan E.S., Fujiki K., Lebon S.,
RA   Cham B., Masuda K., Arakawa M., Jacquinet A., Yamazumi Y., Chen S.T.,
RA   Verloes A., Okada Y., Katou Y., Nakamura T., Akiyama T., Gressens P.,
RA   Foo R., Passemard S., Tan E.C., El Ghouzzi V., Shirahige K.;
RT   "ARCN1 mutations cause a recognizable craniofacial syndrome due to copi-
RT   mediated transport defects.";
RL   Am. J. Hum. Genet. 99:451-459(2016).
CC   -!- FUNCTION: Component of the coatomer, a cytosolic protein complex that
CC       binds to dilysine motifs and reversibly associates with Golgi non-
CC       clathrin-coated vesicles, which further mediate biosynthetic protein
CC       transport from the ER, via the Golgi up to the trans Golgi network. The
CC       coatomer complex is required for budding from Golgi membranes, and is
CC       essential for the retrograde Golgi-to-ER transport of dilysine-tagged
CC       proteins. In mammals, the coatomer can only be recruited by membranes
CC       associated to ADP-ribosylation factors (ARFs), which are small GTP-
CC       binding proteins; the complex also influences the Golgi structural
CC       integrity, as well as the processing, activity, and endocytic recycling
CC       of LDL receptors (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
CC   -!- INTERACTION:
CC       P48444; P53618: COPB1; NbExp=3; IntAct=EBI-1044491, EBI-359063;
CC       P48444; P42858: HTT; NbExp=3; IntAct=EBI-1044491, EBI-466029;
CC       P48444; Q9BQE6-2: LBHD1; NbExp=3; IntAct=EBI-1044491, EBI-12277798;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC       the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P48444-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P48444-2; Sequence=VSP_045636;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DISEASE: Short stature-micrognathia syndrome (SSMG) [MIM:617164]: An
CC       autosomal dominant disorder characterized by facial dysmorphism, severe
CC       micrognathia, microcephaly, rhizomelic short stature, and mild
CC       developmental delay. {ECO:0000269|PubMed:27476655}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry. the
CC       skeletal phenotype, that characterizes this disorder, may be due to
CC       defective type I collagen transport and reduction of collagen
CC       secretion. {ECO:0000269|PubMed:27476655}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       Delta-COP subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA57072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X81197; CAA57071.1; -; mRNA.
DR   EMBL; X81198; CAA57072.1; ALT_INIT; mRNA.
DR   EMBL; AK304019; BAG64934.1; -; mRNA.
DR   EMBL; AP000941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC093636; AAH93636.1; -; mRNA.
DR   EMBL; BC093638; AAH93638.1; -; mRNA.
DR   CCDS; CCDS44749.1; -. [P48444-2]
DR   CCDS; CCDS8400.1; -. [P48444-1]
DR   PIR; A56750; A56750.
DR   RefSeq; NP_001135753.1; NM_001142281.1. [P48444-2]
DR   RefSeq; NP_001646.2; NM_001655.4. [P48444-1]
DR   AlphaFoldDB; P48444; -.
DR   SMR; P48444; -.
DR   BioGRID; 106867; 222.
DR   ComplexPortal; CPX-7803; COPI vesicle coat complex, COPG1-COPZ1 variant.
DR   ComplexPortal; CPX-7969; COPI vesicle coat complex, COPG2-COPZ1 variant.
DR   ComplexPortal; CPX-7970; COPI vesicle coat complex, COPG1-COPZ2 variant.
DR   DIP; DIP-50375N; -.
DR   IntAct; P48444; 69.
DR   MINT; P48444; -.
DR   STRING; 9606.ENSP00000264028; -.
DR   GlyCosmos; P48444; 5 sites, 1 glycan.
DR   GlyGen; P48444; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; P48444; -.
DR   MetOSite; P48444; -.
DR   PhosphoSitePlus; P48444; -.
DR   SwissPalm; P48444; -.
DR   BioMuta; ARCN1; -.
DR   DMDM; 1351970; -.
DR   OGP; P48444; -.
DR   EPD; P48444; -.
DR   jPOST; P48444; -.
DR   MassIVE; P48444; -.
DR   MaxQB; P48444; -.
DR   PaxDb; 9606-ENSP00000264028; -.
DR   PeptideAtlas; P48444; -.
DR   ProteomicsDB; 19961; -.
DR   ProteomicsDB; 55891; -. [P48444-1]
DR   Pumba; P48444; -.
DR   Antibodypedia; 32504; 235 antibodies from 24 providers.
DR   DNASU; 372; -.
DR   Ensembl; ENST00000264028.5; ENSP00000264028.4; ENSG00000095139.15. [P48444-1]
DR   Ensembl; ENST00000392859.7; ENSP00000376599.3; ENSG00000095139.15. [P48444-2]
DR   GeneID; 372; -.
DR   KEGG; hsa:372; -.
DR   MANE-Select; ENST00000264028.5; ENSP00000264028.4; NM_001655.5; NP_001646.2.
DR   UCSC; uc001ptq.4; human. [P48444-1]
DR   AGR; HGNC:649; -.
DR   CTD; 372; -.
DR   DisGeNET; 372; -.
DR   GeneCards; ARCN1; -.
DR   HGNC; HGNC:649; ARCN1.
DR   HPA; ENSG00000095139; Low tissue specificity.
DR   MalaCards; ARCN1; -.
DR   MIM; 600820; gene.
DR   MIM; 617164; phenotype.
DR   neXtProt; NX_P48444; -.
DR   OpenTargets; ENSG00000095139; -.
DR   PharmGKB; PA24931; -.
DR   VEuPathDB; HostDB:ENSG00000095139; -.
DR   eggNOG; KOG2635; Eukaryota.
DR   GeneTree; ENSGT00390000017207; -.
DR   HOGENOM; CLU_019988_2_0_1; -.
DR   InParanoid; P48444; -.
DR   OMA; YDARKHV; -.
DR   OrthoDB; 205756at2759; -.
DR   PhylomeDB; P48444; -.
DR   TreeFam; TF105760; -.
DR   PathwayCommons; P48444; -.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   SignaLink; P48444; -.
DR   BioGRID-ORCS; 372; 799 hits in 1156 CRISPR screens.
DR   ChiTaRS; ARCN1; human.
DR   GenomeRNAi; 372; -.
DR   Pharos; P48444; Tbio.
DR   PRO; PR:P48444; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P48444; Protein.
DR   Bgee; ENSG00000095139; Expressed in islet of Langerhans and 206 other cell types or tissues.
DR   ExpressionAtlas; P48444; baseline and differential.
DR   GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR   GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IEA:Ensembl.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0051645; P:Golgi localization; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR   GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   CDD; cd09254; AP_delta-COPI_MHD; 1.
DR   CDD; cd14830; Delta_COP_N; 1.
DR   Gene3D; 3.30.450.60; -; 1.
DR   Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR   InterPro; IPR036168; AP2_Mu_C_sf.
DR   InterPro; IPR022775; AP_mu_sigma_su.
DR   InterPro; IPR027059; Coatomer_dsu.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR028565; MHD.
DR   PANTHER; PTHR10121; COATOMER SUBUNIT DELTA; 1.
DR   PANTHER; PTHR10121:SF0; COATOMER SUBUNIT DELTA; 1.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   Pfam; PF01217; Clat_adaptor_s; 1.
DR   SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR   SUPFAM; SSF64356; SNARE-like; 1.
DR   PROSITE; PS51072; MHD; 1.
DR   Genevisible; P48444; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW   Dwarfism; ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..511
FT                   /note="Coatomer subunit delta"
FT                   /id="PRO_0000193841"
FT   DOMAIN          271..511
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT   REGION          168..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         233
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         241
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XJY5"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         309
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         351
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XJY5"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..89
FT                   /note="MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETE
FT                   SVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRV -> M (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045636"
FT   VARIANT         186
FT                   /note="F -> L (in dbSNP:rs682327)"
FT                   /id="VAR_011788"
FT   VARIANT         309
FT                   /note="K -> N (in dbSNP:rs1063124)"
FT                   /id="VAR_011789"
FT   CONFLICT        387
FT                   /note="N -> D (in Ref. 2; BAG64934)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  57210 MW;  4ED1F7D2D12A7F75 CRC64;
     MVLLAAAVCT KAGKAIVSRQ FVEMTRTRIE GLLAAFPKLM NTGKQHTFVE TESVRYVYQP
     MEKLYMVLIT TKNSNILEDL ETLRLFSRVI PEYCRALEEN EISEHCFDLI FAFDEIVALG
     YRENVNLAQI RTFTEMDSHE EKVFRAVRET QEREAKAEMR RKAKELQQAR RDAERQGKKA
     PGFGGFGSSA VSGGSTAAMI TETIIETDKP KVAPAPARPS GPSKALKLGA KGKEVDNFVD
     KLKSEGETIM SSSMGKRTSE ATKMHAPPIN MESVHMKIEE KITLTCGRDG GLQNMELHGM
     IMLRISDDKY GRIRLHVENE DKKGVQLQTH PNVDKKLFTA ESLIGLKNPE KSFPVNSDVG
     VLKWRLQTTE ESFIPLTINC WPSESGNGCD VNIEYELQED NLELNDVVIT IPLPSGVGAP
     VIGEIDGEYR HDSRRNTLEW CLPVIDAKNK SGSLEFSIAG QPNDFFPVQV SFVSKKNYCN
     IQVTKVTQVD GNSPVRFSTE TTFLVDKYEI L
//