TMCC2_HUMAN
ID TMCC2_HUMAN Reviewed; 709 AA.
AC O75069; A2RRH3; B2RAX5; B3KTM7; B7Z1P7; Q6ZN09; Q7Z6C6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Transmembrane and coiled-coil domains protein 2 {ECO:0000303|PubMed:21593558};
DE AltName: Full=Cerebral protein 11 {ECO:0000303|Ref.2};
GN Name=TMCC2 {ECO:0000303|PubMed:21593558};
GN Synonyms=KIAA0481 {ECO:0000303|PubMed:9455484};
GN ORFNames=hucep-11 {ECO:0000303|Ref.2};
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).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RA Yoshimoto M., Yazaki M., Takayama K., Matsumoto K., Tsuritani K.;
RT "Molecular cloning of a gene specifically expressed in human central
RT nervous system.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5).
RC TISSUE=Brain, and Cerebellum;
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 [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 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP INTERACTION WITH APOE AND APP C99, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21593558; DOI=10.3233/jad-2011-102115;
RA Hopkins P.C., Sainz-Fuertes R., Lovestone S.;
RT "The impact of a novel apolipoprotein E and amyloid-beta protein precursor-
RT interacting protein on the production of amyloid-beta.";
RL J. Alzheimers Dis. 26:239-253(2011).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP 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: May be involved in the regulation of the proteolytic
CC processing of the amyloid precursor protein (APP) possibly also
CC implicating APOE. {ECO:0000269|PubMed:21593558}.
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). Interacts with APOE and
CC proteolytic processed C-terminal fragment C99 of the amyloid precursor
CC protein (APP C99) (PubMed:21593558). {ECO:0000269|PubMed:21593558,
CC ECO:0000269|PubMed:24454821}.
CC -!- INTERACTION:
CC O75069; P02649: APOE; NbExp=5; IntAct=EBI-726731, EBI-1222467;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21593558, ECO:0000269|PubMed:24454821,
CC ECO:0000269|PubMed:30220460}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Concentrates in discrete patches along peripheral
CC endoplasmic reticulum tubules. {ECO:0000269|PubMed:30220460}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75069-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75069-2; Sequence=VSP_046245;
CC Name=3;
CC IsoId=O75069-3; Sequence=VSP_058939;
CC Name=5;
CC IsoId=O75069-5; Sequence=VSP_058940;
CC -!- SIMILARITY: Belongs to the TEX28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53876.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. The N-terminus part of this cDNA matches at different locus on chromosome 1.; Evidence={ECO:0000305};
CC Sequence=BAA32326.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB007950; BAA32326.3; ALT_INIT; mRNA.
DR EMBL; AB001596; BAB46924.1; -; mRNA.
DR EMBL; AK095816; BAG53139.1; -; mRNA.
DR EMBL; AK131419; BAD18566.1; -; mRNA.
DR EMBL; AK293734; BAH11583.1; -; mRNA.
DR EMBL; AK314398; BAG37022.1; -; mRNA.
DR EMBL; AC093422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91548.1; -; Genomic_DNA.
DR EMBL; BC053876; AAH53876.1; ALT_SEQ; mRNA.
DR EMBL; BC131629; AAI31630.1; -; mRNA.
DR CCDS; CCDS30984.1; -. [O75069-1]
DR CCDS; CCDS55676.1; -. [O75069-2]
DR CCDS; CCDS73010.1; -. [O75069-3]
DR CCDS; CCDS76257.1; -. [O75069-5]
DR RefSeq; NP_001229854.1; NM_001242925.1. [O75069-2]
DR RefSeq; NP_001284540.1; NM_001297611.1. [O75069-5]
DR RefSeq; NP_001284542.1; NM_001297613.1. [O75069-3]
DR RefSeq; NP_055673.2; NM_014858.3. [O75069-1]
DR RefSeq; XP_005245741.1; XM_005245684.1.
DR RefSeq; XP_005245742.1; XM_005245685.4.
DR AlphaFoldDB; O75069; -.
DR SMR; O75069; -.
DR BioGRID; 115240; 46.
DR IntAct; O75069; 19.
DR MINT; O75069; -.
DR STRING; 9606.ENSP00000350718; -.
DR iPTMnet; O75069; -.
DR PhosphoSitePlus; O75069; -.
DR BioMuta; TMCC2; -.
DR EPD; O75069; -.
DR jPOST; O75069; -.
DR MassIVE; O75069; -.
DR MaxQB; O75069; -.
DR PaxDb; O75069; -.
DR PeptideAtlas; O75069; -.
DR PRIDE; O75069; -.
DR ProteomicsDB; 49736; -. [O75069-1]
DR ProteomicsDB; 6357; -.
DR Antibodypedia; 2865; 53 antibodies from 18 providers.
DR DNASU; 9911; -.
DR Ensembl; ENST00000329800.7; ENSP00000329436.6; ENSG00000133069.17. [O75069-3]
DR Ensembl; ENST00000358024.8; ENSP00000350718.3; ENSG00000133069.17. [O75069-1]
DR Ensembl; ENST00000545499.5; ENSP00000437943.1; ENSG00000133069.17. [O75069-2]
DR Ensembl; ENST00000637895.1; ENSP00000490308.1; ENSG00000133069.17. [O75069-5]
DR GeneID; 9911; -.
DR KEGG; hsa:9911; -.
DR MANE-Select; ENST00000358024.8; ENSP00000350718.3; NM_014858.4; NP_055673.2.
DR UCSC; uc001hca.4; human. [O75069-1]
DR CTD; 9911; -.
DR DisGeNET; 9911; -.
DR GeneCards; TMCC2; -.
DR HGNC; HGNC:24239; TMCC2.
DR HPA; ENSG00000133069; Group enriched (bone marrow, brain).
DR MIM; 619429; gene.
DR neXtProt; NX_O75069; -.
DR OpenTargets; ENSG00000133069; -.
DR PharmGKB; PA134963344; -.
DR VEuPathDB; HostDB:ENSG00000133069; -.
DR eggNOG; KOG3850; Eukaryota.
DR GeneTree; ENSGT00940000158314; -.
DR HOGENOM; CLU_019951_1_0_1; -.
DR InParanoid; O75069; -.
DR OrthoDB; 1175041at2759; -.
DR PhylomeDB; O75069; -.
DR TreeFam; TF316292; -.
DR PathwayCommons; O75069; -.
DR SignaLink; O75069; -.
DR BioGRID-ORCS; 9911; 18 hits in 1077 CRISPR screens.
DR ChiTaRS; TMCC2; human.
DR GenomeRNAi; 9911; -.
DR Pharos; O75069; Tdark.
DR PRO; PR:O75069; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75069; protein.
DR Bgee; ENSG00000133069; Expressed in C1 segment of cervical spinal cord and 149 other tissues.
DR ExpressionAtlas; O75069; baseline and differential.
DR Genevisible; O75069; HS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; 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 Alternative splicing; Coiled coil; Endoplasmic reticulum; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..709
FT /note="Transmembrane and coiled-coil domains protein 2"
FT /id="PRO_0000184597"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..368
FT /evidence="ECO:0000255"
FT COILED 514..633
FT /evidence="ECO:0000255"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W04"
FT MOD_RES 163
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q80W04"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W04"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W04"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W04"
FT VAR_SEQ 1..249
FT /note="MKRCRSDELQQQQGEEDGAGLEDAASHLPGADLRPGETTGANSAGGPTSDAG
FT AAAAPNPGPRSKPPDLKKIQQLSEGSMFGHGLKHLFHSRRRSREREHQTSQDSQQHQQQ
FT QGMSDHDSPDEKERSPEMHRVSYAMSLHDLPARPTAFNRVLQQIRSRPSIKRGASLHSS
FT SGGGSSGSSSRRTKSSSLEPQRGSPHLLRKAPQDSSLAAILHQHQCRPRSSSTTDTALL
FT LADGSNVYLLAEEAEGIGDK -> MKSKEEETA (in isoform 3)"
FT /id="VSP_058939"
FT VAR_SEQ 1..249
FT /note="MKRCRSDELQQQQGEEDGAGLEDAASHLPGADLRPGETTGANSAGGPTSDAG
FT AAAAPNPGPRSKPPDLKKIQQLSEGSMFGHGLKHLFHSRRRSREREHQTSQDSQQHQQQ
FT QGMSDHDSPDEKERSPEMHRVSYAMSLHDLPARPTAFNRVLQQIRSRPSIKRGASLHSS
FT SGGGSSGSSSRRTKSSSLEPQRGSPHLLRKAPQDSSLAAILHQHQCRPRSSSTTDTALL
FT LADGSNVYLLAEEAEGIGDK -> MNQVVQPLMSRHSACRGSQAHLSW (in
FT isoform 5)"
FT /id="VSP_058940"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046245"
FT CONFLICT 466
FT /note="T -> A (in Ref. 5; BAG53139)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="S -> I (in Ref. 5; BAG37022)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="N -> Y (in Ref. 5; BAG37022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 77449 MW; 002993EA6B0E4546 CRC64;
MKRCRSDELQ QQQGEEDGAG LEDAASHLPG ADLRPGETTG ANSAGGPTSD AGAAAAPNPG
PRSKPPDLKK IQQLSEGSMF GHGLKHLFHS RRRSREREHQ TSQDSQQHQQ QQGMSDHDSP
DEKERSPEMH RVSYAMSLHD LPARPTAFNR VLQQIRSRPS IKRGASLHSS SGGGSSGSSS
RRTKSSSLEP QRGSPHLLRK APQDSSLAAI LHQHQCRPRS SSTTDTALLL ADGSNVYLLA
EEAEGIGDKV DKGDLVALSL PAGHGDTDGP ISLDVPDGAP DPQRTKAAID HLHQKILKIT
EQIKIEQEAR DDNVAEYLKL ANNADKQQVS RIKQVFEKKN QKSAQTIAQL HKKLEHYRRR
LKEIEQNGPS RQPKDVLRDM QQGLKDVGAN VRAGISGFGG GVVEGVKGSL SGLSQATHTA
VVSKPREFAS LIRNKFGSAD NIAHLKDPLE DGPPEEAARA LSGSATLVSS PKYGSDDECS
SASASSAGAG SNSGAGPGGA LGSPKSNALY GAPGNLDALL EELREIKEGQ SHLEDSMEDL
KTQLQRDYTY MTQCLQEERY RYERLEEQLN DLTELHQNEM TNLKQELASM EEKVAYQSYE
RARDIQEAVE SCLTRVTKLE LQQQQQQVVQ LEGVENANAR ALLGKFINVI LALMAVLLVF
VSTIANFITP LMKTRLRITS TTLLVLVLFL LWKHWDSLTY LLEHVLLPS
