TMCC1_HUMAN
ID TMCC1_HUMAN Reviewed; 653 AA.
AC O94876; A8K5Y3; B4DE04; Q68E06; Q8IXM8;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Transmembrane and coiled-coil domains protein 1 {ECO:0000303|PubMed:24454821};
GN Name=TMCC1 {ECO:0000303|PubMed:24454821, ECO:0000312|HGNC:HGNC:29116};
GN Synonyms=KIAA0779 {ECO:0000303|PubMed:9872452};
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] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-165.
RC TISSUE=Brain, and Urinary bladder;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-165.
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-653 (ISOFORM 1), AND VARIANT
RP GLY-165.
RC TISSUE=Endometrial tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-653 (ISOFORM 1/2).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, VARIANT [LARGE SCALE
RP ANALYSIS] GLY-165, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-414, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP 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 SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=24454821; DOI=10.1371/journal.pone.0085206;
RA Zhang C., Kho Y.S., Wang Z., Chiang Y.T., Ng G.K., Shaw P.C., Wang Y.,
RA Qi R.Z.;
RT "Transmembrane and coiled-coil domain family 1 is a novel protein of the
RT endoplasmic reticulum.";
RL PLoS ONE 9:E85206-E85206(2014).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30220460; DOI=10.1016/j.cell.2018.08.030;
RA Hoyer M.J., Chitwood P.J., Ebmeier C.C., Striepen J.F., Qi R.Z., Old W.M.,
RA Voeltz G.K.;
RT "A novel class of ER membrane proteins regulates ER-associated endosome
RT fission.";
RL Cell 175:254-265(2018).
CC -!- FUNCTION: Endoplasmic reticulum membrane protein that promotes
CC endoplasmic reticulum-associated endosome fission (PubMed:30220460).
CC Localizes to contact sites between the endoplasmic reticulum and
CC endosomes and acts by promoting recruitment of the endoplasmic
CC reticulum to endosome tubules for fission (PubMed:30220460). Endosome
CC membrane fission of early and late endosomes is essential to separate
CC regions destined for lysosomal degradation from carriers to be recycled
CC to the plasma membrane (PubMed:30220460).
CC {ECO:0000269|PubMed:30220460}.
CC -!- SUBUNIT: May form homodimers and heterodimers with TMCC2 or TMCC3 via
CC the coiled-coil domains (PubMed:24454821). Interacts with ribosomal
CC proteins RPL4 and RPS6 (PubMed:24454821).
CC {ECO:0000269|PubMed:24454821}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24454821, ECO:0000269|PubMed:30220460}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Specifically localizes to contact
CC sites between the endoplasmic reticulum and endosomes that are
CC spatially and temporally linked to endosome fission.
CC {ECO:0000269|PubMed:30220460}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94876-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94876-2; Sequence=VSP_053924, VSP_053925;
CC -!- SIMILARITY: Belongs to the TEX28 family. {ECO:0000305}.
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DR EMBL; AK291448; BAF84137.1; -; mRNA.
DR EMBL; AK293408; BAG56915.1; -; mRNA.
DR EMBL; AC023162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039859; AAH39859.1; -; mRNA.
DR EMBL; CR749206; CAH18064.2; -; mRNA.
DR EMBL; AB018322; BAA34499.1; -; mRNA.
DR CCDS; CCDS33855.1; -. [O94876-1]
DR RefSeq; NP_001017395.2; NM_001017395.3. [O94876-1]
DR RefSeq; NP_001121696.1; NM_001128224.2.
DR RefSeq; XP_006713605.1; XM_006713542.3.
DR RefSeq; XP_006713606.1; XM_006713543.3.
DR RefSeq; XP_006713607.1; XM_006713544.1. [O94876-1]
DR RefSeq; XP_011510874.1; XM_011512572.2.
DR RefSeq; XP_011510875.1; XM_011512573.2. [O94876-1]
DR RefSeq; XP_011510878.1; XM_011512576.2.
DR RefSeq; XP_011510881.1; XM_011512579.2.
DR RefSeq; XP_011510884.1; XM_011512582.1.
DR RefSeq; XP_016861420.1; XM_017005931.1. [O94876-1]
DR RefSeq; XP_016861421.1; XM_017005932.1.
DR RefSeq; XP_016861422.1; XM_017005933.1. [O94876-1]
DR AlphaFoldDB; O94876; -.
DR BioGRID; 116663; 19.
DR IntAct; O94876; 10.
DR MINT; O94876; -.
DR STRING; 9606.ENSP00000376930; -.
DR iPTMnet; O94876; -.
DR PhosphoSitePlus; O94876; -.
DR BioMuta; TMCC1; -.
DR EPD; O94876; -.
DR jPOST; O94876; -.
DR MassIVE; O94876; -.
DR MaxQB; O94876; -.
DR PaxDb; O94876; -.
DR PeptideAtlas; O94876; -.
DR PRIDE; O94876; -.
DR ProteomicsDB; 50519; -. [O94876-1]
DR Antibodypedia; 33295; 114 antibodies from 19 providers.
DR DNASU; 23023; -.
DR Ensembl; ENST00000393238.8; ENSP00000376930.3; ENSG00000172765.18. [O94876-1]
DR GeneID; 23023; -.
DR KEGG; hsa:23023; -.
DR MANE-Select; ENST00000393238.8; ENSP00000376930.3; NM_001017395.5; NP_001017395.2.
DR UCSC; uc021xdy.2; human. [O94876-1]
DR CTD; 23023; -.
DR DisGeNET; 23023; -.
DR GeneCards; TMCC1; -.
DR HGNC; HGNC:29116; TMCC1.
DR HPA; ENSG00000172765; Low tissue specificity.
DR MIM; 616242; gene.
DR neXtProt; NX_O94876; -.
DR OpenTargets; ENSG00000172765; -.
DR PharmGKB; PA134951990; -.
DR VEuPathDB; HostDB:ENSG00000172765; -.
DR eggNOG; KOG3850; Eukaryota.
DR GeneTree; ENSGT00940000155189; -.
DR InParanoid; O94876; -.
DR OMA; QADMEPE; -.
DR OrthoDB; 1175041at2759; -.
DR PhylomeDB; O94876; -.
DR TreeFam; TF316292; -.
DR PathwayCommons; O94876; -.
DR SignaLink; O94876; -.
DR BioGRID-ORCS; 23023; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; TMCC1; human.
DR GenomeRNAi; 23023; -.
DR Pharos; O94876; Tbio.
DR PRO; PR:O94876; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O94876; protein.
DR Bgee; ENSG00000172765; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; O94876; baseline and differential.
DR Genevisible; O94876; HS.
DR GO; GO:0005829; C:cytosol; IMP:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140284; C:endoplasmic reticulum-endosome membrane contact site; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IDA:UniProtKB.
DR GO; GO:0140285; P:endosome fission; IDA:UniProtKB.
DR GO; GO:0097750; P:endosome membrane tubulation; IDA:UniProtKB.
DR GO; GO:0090148; P:membrane fission; IDA:UniProtKB.
DR InterPro; IPR019394; TEX28/TMCC.
DR PANTHER; PTHR17613; PTHR17613; 1.
DR Pfam; PF10267; Tmemb_cc2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..653
FT /note="Transmembrane and coiled-coil domains protein 1"
FT /id="PRO_0000184595"
FT TOPO_DOM 1..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 228..313
FT /evidence="ECO:0000255"
FT COILED 458..576
FT /evidence="ECO:0000255"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..13
FT /note="MEPSGSEQLFEDP -> MVQRFSLRRQLSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053924"
FT VAR_SEQ 14..192
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053925"
FT VARIANT 165
FT /note="S -> G (in dbSNP:rs784689)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0007744|PubMed:19690332"
FT /id="VAR_047918"
FT CONFLICT 166
FT /note="S -> T (in Ref. 1; BAF84137)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="D -> G (in Ref. 1; BAF84137)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 72083 MW; B9C3A26AE9583FF2 CRC64;
MEPSGSEQLF EDPDPGGKSQ DAEARKQTES EQKLSKMTHN ALENINVIGQ GLKHLFQHQR
RRSSVSPHDV QQIQADPEPE MDLESQNACA EIDGVPTHPT ALNRVLQQIR VPPKMKRGTS
LHSRRGKPEA PKGSPQINRK SGQEMTAVMQ SGRPRSSSTT DAPTSSAMME IACAAAAAAA
ACLPGEEGTA ERIERLEVSS LAQTSSAVAS STDGSIHTDS VDGTPDPQRT KAAIAHLQQK
ILKLTEQIKI AQTARDDNVA EYLKLANSAD KQQAARIKQV FEKKNQKSAQ TILQLQKKLE
HYHRKLREVE QNGIPRQPKD VFRDMHQGLK DVGAKVTGFS EGVVDSVKGG FSSFSQATHS
AAGAVVSKPR EIASLIRNKF GSADNIPNLK DSLEEGQVDD AGKALGVISN FQSSPKYGSE
EDCSSATSGS VGANSTTGGI AVGASSSKTN TLDMQSSGFD ALLHEIQEIR ETQARLEESF
ETLKEHYQRD YSLIMQTLQE ERYRCERLEE QLNDLTELHQ NEILNLKQEL ASMEEKIAYQ
SYERARDIQE ALEACQTRIS KMELQQQQQQ VVQLEGLENA TARNLLGKLI NILLAVMAVL
LVFVSTVANC VVPLMKTRNR TFSTLFLVVF IAFLWKHWDA LFSYVERFFS SPR
