RBCC

ESYT2 (FAM62B, KIAA1228) [Confidence: high (present in two of the MS resources)]
Extended synaptotagmin-2; E-Syt2 (Chr2Syt)

hRBCD IPI00409635
IPI00409635 KIAA1228 protein no information available soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight

Comments
Isoform A0FGR8-2 was detected.

UniProt A0FGR8
ID ESYT2_HUMAN Reviewed; 921 AA.
AC A0FGR8; A4D229; Q69YJ2; Q6UKI4; Q6ZTU0; Q6ZVU1; Q9BQS0; Q9NW47;
read moreAC Q9ULJ2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 22-JAN-2014, entry version 74.
DE RecName: Full=Extended synaptotagmin-2;
DE Short=E-Syt2;
DE AltName: Full=Chr2Syt;
GN Name=ESYT2; Synonyms=FAM62B, KIAA1228;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17360437; DOI=10.1073/pnas.0611725104;
RA Min S.-W., Chang W.-P., Suedhof T.C.;
RT "E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2
RT domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3823-3828(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Shan Y.X., Yu L.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 511-921 (ISOFORMS 1/2), AND VARIANT
RP GLY-638.
RC TISSUE=Esophageal carcinoma, and Thymus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-921 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-921.
RC TISSUE=Melanoma;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-921 (ISOFORM 6).
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 747-904.
RC TISSUE=Brain;
RX PubMed=11543631; DOI=10.1006/geno.2001.6619;
RA Craxton M.A.;
RT "Genomic analysis of synaptotagmin genes.";
RL Genomics 77:43-49(2001).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-758 AND
RP SER-761, AND MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-755; SER-758
RP AND SER-761, AND MASS SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691; SER-739; SER-748;
RP SER-755; SER-758 AND SER-761, AND MASS SPECTROMETRY.
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-758 AND
RP SER-761, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND SER-761, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP STRUCTURE BY NMR OF 222-350.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the third C2 domain of KIAA1228 protein.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: May play a role as calcium-regulated intrinsic membrane
CC protein.
CC -!- INTERACTION:
CC Q9BSJ8:ESYT1; NbExp=4; IntAct=EBI-3184170, EBI-355956;
CC A0FGR9:ESYT3; NbExp=3; IntAct=EBI-3184170, EBI-8771391;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=A0FGR8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0FGR8-2; Sequence=VSP_023239;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=A0FGR8-4; Sequence=VSP_023238, VSP_023241, VSP_023242;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=A0FGR8-5; Sequence=VSP_023236, VSP_023240;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=A0FGR8-6; Sequence=VSP_038324;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with high level in
CC cerebellum.
CC -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC -!- SIMILARITY: Contains 3 C2 domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91539.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC85769.1; Type=Frameshift; Positions=800;
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DR EMBL; DQ993201; ABJ97706.1; -; mRNA.
DR EMBL; AY368150; AAR89381.1; -; mRNA.
DR EMBL; AK001181; BAA91539.1; ALT_INIT; mRNA.
DR EMBL; AK124091; BAC85769.1; ALT_FRAME; mRNA.
DR EMBL; AK126214; BAC86489.1; -; mRNA.
DR EMBL; CH236954; EAL23931.1; -; Genomic_DNA.
DR EMBL; AB033054; BAA86542.2; -; mRNA.
DR EMBL; AL833233; CAH10642.1; -; mRNA.
DR EMBL; BC013957; AAH13957.2; -; mRNA.
DR EMBL; AJ303365; CAC33887.1; -; mRNA.
DR RefSeq; NP_065779.1; NM_020728.2.
DR RefSeq; XP_005249608.1; XM_005249551.1.
DR UniGene; Hs.490795; -.
DR PDB; 2DMG; NMR; -; A=785-913.
DR PDBsum; 2DMG; -.
DR ProteinModelPortal; A0FGR8; -.
DR SMR; A0FGR8; 385-479, 756-919.
DR IntAct; A0FGR8; 8.
DR MINT; MINT-4541681; -.
DR PhosphoSite; A0FGR8; -.
DR PaxDb; A0FGR8; -.
DR PRIDE; A0FGR8; -.
DR DNASU; 57488; -.
DR Ensembl; ENST00000251527; ENSP00000251527; ENSG00000117868.
DR GeneID; 57488; -.
DR KEGG; hsa:57488; -.
DR UCSC; uc003woc.1; human.
DR CTD; 57488; -.
DR GeneCards; GC07M158523; -.
DR H-InvDB; HIX0007266; -.
DR HGNC; HGNC:22211; ESYT2.
DR HPA; HPA002132; -.
DR neXtProt; NX_A0FGR8; -.
DR PharmGKB; PA165617947; -.
DR eggNOG; COG5038; -.
DR HOVERGEN; HBG055795; -.
DR InParanoid; A0FGR8; -.
DR OMA; VDVGQQP; -.
DR OrthoDB; EOG7RNJZK; -.
DR ChiTaRS; ESYT2; human.
DR EvolutionaryTrace; A0FGR8; -.
DR GeneWiki; FAM62B; -.
DR GenomeRNAi; 57488; -.
DR NextBio; 63768; -.
DR PRO; PR:A0FGR8; -.
DR ArrayExpress; A0FGR8; -.
DR Bgee; A0FGR8; -.
DR CleanEx; HS_FAM62B; -.
DR Genevestigator; A0FGR8; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR000008; C2_dom.
DR Pfam; PF00168; C2; 3.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; SSF49562; 3.
DR PROSITE; PS50004; C2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 921 Extended synaptotagmin-2.
FT /FTId=PRO_0000278258.
FT TRANSMEM 128 148 Helical; (Potential).
FT TRANSMEM 302 322 Helical; (Potential).
FT DOMAIN 372 473 C2 1.
FT DOMAIN 523 617 C2 2.
FT DOMAIN 788 892 C2 3.
FT COMPBIAS 736 739 Poly-Ser.
FT MOD_RES 691 691 Phosphoserine.
FT MOD_RES 738 738 Phosphoserine (By similarity).
FT MOD_RES 739 739 Phosphoserine.
FT MOD_RES 743 743 Phosphoserine.
FT MOD_RES 748 748 Phosphoserine.
FT MOD_RES 755 755 Phosphoserine.
FT MOD_RES 758 758 Phosphoserine.
FT MOD_RES 761 761 Phosphoserine.
FT VAR_SEQ 1 593 Missing (in isoform 5).
FT /FTId=VSP_023236.
FT VAR_SEQ 1 204 Missing (in isoform 4).
FT /FTId=VSP_023238.
FT VAR_SEQ 1 97 MTANRDAALSSHRHPGCAQRPRTPTFASSSQRRSAFGFDDG
FT NFPGLGERSHAPGSRLGARRRAKTARGLRGHRQRGAGAGLS
FT RPGSARAPSPPRPGG -> MTPPSRAEAGVRRSRVPSEGRW
FT RGAEPPGISASTQPASAGRAARHCGAMSGARGEGPEAGAGG
FT AGGRAA (in isoform 2).
FT /FTId=VSP_023239.
FT VAR_SEQ 550 550 S -> SNPLEFNPDVLKKTAVQRALKS (in isoform
FT 6).
FT /FTId=VSP_038324.
FT VAR_SEQ 594 603 NPKRQDLEVE -> MPVLPPCVLQ (in isoform 5).
FT /FTId=VSP_023240.
FT VAR_SEQ 706 731 PVIGGSDKPGMEEKAQPPEAGPQGLH -> SQSRSRPPASP
FT RTSRCPSPPRSCGKG (in isoform 4).
FT /FTId=VSP_023241.
FT VAR_SEQ 732 921 Missing (in isoform 4).
FT /FTId=VSP_023242.
FT VARIANT 210 210 C -> S (in dbSNP:rs13233513).
FT /FTId=VAR_030725.
FT VARIANT 638 638 S -> G (in dbSNP:rs2305473).
FT /FTId=VAR_030726.
FT CONFLICT 141 141 L -> V (in Ref. 7; CAH10642).
FT CONFLICT 612 612 S -> P (in Ref. 3; BAC85769).
FT CONFLICT 615 615 N -> S (in Ref. 3; BAC86489).
FT CONFLICT 795 795 R -> Q (in Ref. 3; BAC85769).
FT STRAND 789 797
FT TURN 798 801
FT STRAND 802 811
FT STRAND 823 831
FT STRAND 835 837
FT STRAND 851 858
FT HELIX 862 867
FT STRAND 869 876
FT STRAND 889 894
FT TURN 899 902
SQ SEQUENCE 921 AA; 102357 MW; D57F1BD9BB0A0C8A CRC64;
MTANRDAALS SHRHPGCAQR PRTPTFASSS QRRSAFGFDD GNFPGLGERS HAPGSRLGAR
RRAKTARGLR GHRQRGAGAG LSRPGSARAP SPPRPGGPEN PGGVLSVELP GLLAQLARSF
ALLLPVYALG YLGLSFSWVL LALALLAWCR RSRGLKALRL CRALALLEDE ERVVRLGVRA
CDLPAWVHFP DTERAEWLNK TVKHMWPFIC QFIEKLFRET IEPAVRGANT HLSTFSFTKV
DVGQQPLRIN GVKVYTENVD KRQIILDLQI SFVGNCEIDL EIKRYFCRAG VKSIQIHGTM
RVILEPLIGD MPLVGALSIF FLRKPLLEIN WTGLTNLLDV PGLNGLSDTI ILDIISNYLV
LPNRITVPLV SEVQIAQLRF PVPKGVLRIH FIEAQDLQGK DTYLKGLVKG KSDPYGIIRV
GNQIFQSRVI KENLSPKWNE VYEALVYEHP GQELEIELFD EDPDKDDFLG SLMIDLIEVE
KERLLDEWFT LDEVPKGKLH LRLEWLTLMP NASNLDKVLT DIKADKDQAN DGLSSALLIL
YLDSARNLPS GKKISSNPNP VVQMSVGHKA QESKIRYKTN EPVWEENFTF FIHNPKRQDL
EVEVRDEQHQ CSLGNLKVPL SQLLTSEDMT VSQRFQLSNS GPNSTIKMKI ALRVLHLEKR
ERPPDHQHSA QVKRPSVSKE GRKTSIKSHM SGSPGPGGSN TAPSTPVIGG SDKPGMEEKA
QPPEAGPQGL HDLGRSSSSL LASPGHISVK EPTPSIASDI SLPIATQELR QRLRQLENGT
TLGQSPLGQI QLTIRHSSQR NKLIVVVHAC RNLIAFSEDG SDPYVRMYLL PDKRRSGRRK
THVSKKTLNP VFDQSFDFSV SLPEVQRRTL DVAVKNSGGF LSKDKGLLGK VLVALASEEL
AKGWTQWYDL TEDGTRPQAM T
//

RBCC Red Blood Cell Collection

Full text data of ESYT2