PROM2_HUMAN
ID PROM2_HUMAN Reviewed; 834 AA.
AC Q8N271; A8K2V1; Q2HIX6; Q8NB84; Q8TAE2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Prominin-2;
DE Short=PROM-2;
DE AltName: Full=Prominin-like protein 2;
DE Short=hPROML2;
DE Flags: Precursor;
GN Name=PROM2; Synonyms=PROML2; ORFNames=UNQ2521/PRO6014;
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), TISSUE SPECIFICITY, AND VARIANT
RP ARG-508.
RC TISSUE=Kidney;
RX PubMed=12514187; DOI=10.1074/jbc.m210640200;
RA Fargeas C.A., Florek M., Huttner W.B., Corbeil D.;
RT "Characterization of prominin-2, a new member of the prominin family of
RT pentaspan membrane glycoproteins.";
RL J. Biol. Chem. 278:8586-8596(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-508.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 433-834 (ISOFORM 2).
RC TISSUE=Brain, and Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-508.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ARG-508.
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=12446606; DOI=10.1210/en.2002-220522;
RA Zhang Q., Haleem R., Cai X., Wang Z.;
RT "Identification and characterization of a novel testosterone-regulated
RT prominin-like gene in the rat ventral prostate.";
RL Endocrinology 143:4788-4796(2002).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16673119; DOI=10.1007/s00428-006-0210-9;
RA Mori T., Orikasa H., Shigematsu T., Yamazaki K.;
RT "An ultrastructural and immunohistochemical study of a combined submucosal
RT granular cell tumor and lipoma of the colon showing a unique nodule-in-
RT nodule structure: putative implication of CD34 or prominin-2-positive
RT stromal cells in its histopathogenesis.";
RL Virchows Arch. 449:137-139(2006).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=17874118; DOI=10.1007/s00418-007-0334-2;
RA Jaszai J., Janich P., Farkas L.M., Fargeas C.A., Huttner W.B., Corbeil D.;
RT "Differential expression of prominin-1 (CD133) and prominin-2 in major
RT cephalic exocrine glands of adult mice.";
RL Histochem. Cell Biol. 128:409-419(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- SUBUNIT: Binds cholesterol. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N271; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-18210782, EBI-19125216;
CC Q8N271; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-18210782, EBI-13345167;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
CC projection, microvillus membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Note=Colocalizes with PROM1.
CC Associates with membrane in a cholesterol-dependent manner. Localizes
CC to the apical and basolateral membranes of epithelial cells (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N271-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N271-2; Sequence=VSP_033149;
CC Name=3;
CC IsoId=Q8N271-3; Sequence=VSP_033148;
CC -!- TISSUE SPECIFICITY: Present in saliva within small membrane particles
CC (at protein level). Expressed in kidney, prostate, trachea, esophagus,
CC salivary gland, thyroid gland, mammary gland adrenal gland, placenta,
CC stomach, spinal cord and liver. In submucosal tumor, expressed in
CC spindle-shaped or stellate stromal cells. Expressed in prostate cancer
CC cell lines. {ECO:0000269|PubMed:12446606, ECO:0000269|PubMed:12514187,
CC ECO:0000269|PubMed:16673119, ECO:0000269|PubMed:17874118}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prominin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03657.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF245303; AAM10541.1; -; mRNA.
DR EMBL; AF245304; AAM10542.1; -; mRNA.
DR EMBL; AY358377; AAQ88743.1; -; mRNA.
DR EMBL; AK091175; BAC03599.1; -; mRNA.
DR EMBL; AK091408; BAC03657.1; ALT_INIT; mRNA.
DR EMBL; AK290366; BAF83055.1; -; mRNA.
DR EMBL; AC009238; AAY14751.1; -; Genomic_DNA.
DR EMBL; CH471219; EAX10718.1; -; Genomic_DNA.
DR EMBL; BC113877; AAI13878.1; -; mRNA.
DR EMBL; BC114525; AAI14526.1; -; mRNA.
DR CCDS; CCDS2012.1; -. [Q8N271-1]
DR RefSeq; NP_001159449.1; NM_001165977.2. [Q8N271-1]
DR RefSeq; NP_001159450.1; NM_001165978.2. [Q8N271-1]
DR RefSeq; NP_653308.2; NM_144707.3. [Q8N271-1]
DR AlphaFoldDB; Q8N271; -.
DR BioGRID; 127318; 6.
DR IntAct; Q8N271; 3.
DR MINT; Q8N271; -.
DR STRING; 9606.ENSP00000318270; -.
DR TCDB; 9.B.411.1.2; the prominin (prominin) family.
DR GlyConnect; 1643; 6 N-Linked glycans (2 sites).
DR GlyGen; Q8N271; 4 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; Q8N271; -.
DR PhosphoSitePlus; Q8N271; -.
DR BioMuta; PROM2; -.
DR DMDM; 74728673; -.
DR EPD; Q8N271; -.
DR jPOST; Q8N271; -.
DR MassIVE; Q8N271; -.
DR MaxQB; Q8N271; -.
DR PaxDb; Q8N271; -.
DR PeptideAtlas; Q8N271; -.
DR PRIDE; Q8N271; -.
DR ProteomicsDB; 71663; -. [Q8N271-1]
DR ProteomicsDB; 71664; -. [Q8N271-2]
DR ProteomicsDB; 71665; -. [Q8N271-3]
DR Antibodypedia; 54175; 327 antibodies from 28 providers.
DR DNASU; 150696; -.
DR Ensembl; ENST00000317620.14; ENSP00000318270.9; ENSG00000155066.16. [Q8N271-1]
DR Ensembl; ENST00000317668.8; ENSP00000318520.4; ENSG00000155066.16. [Q8N271-1]
DR Ensembl; ENST00000403131.6; ENSP00000385716.2; ENSG00000155066.16. [Q8N271-1]
DR GeneID; 150696; -.
DR KEGG; hsa:150696; -.
DR MANE-Select; ENST00000317620.14; ENSP00000318270.9; NM_001165978.3; NP_001159450.1.
DR UCSC; uc002suh.3; human. [Q8N271-1]
DR CTD; 150696; -.
DR DisGeNET; 150696; -.
DR GeneCards; PROM2; -.
DR HGNC; HGNC:20685; PROM2.
DR HPA; ENSG00000155066; Tissue enhanced (esophagus, skin).
DR neXtProt; NX_Q8N271; -.
DR OpenTargets; ENSG00000155066; -.
DR PharmGKB; PA134861956; -.
DR VEuPathDB; HostDB:ENSG00000155066; -.
DR eggNOG; KOG4331; Eukaryota.
DR GeneTree; ENSGT00530000063586; -.
DR HOGENOM; CLU_008293_2_0_1; -.
DR InParanoid; Q8N271; -.
DR OMA; VKEQMEP; -.
DR OrthoDB; 1129032at2759; -.
DR PhylomeDB; Q8N271; -.
DR TreeFam; TF324631; -.
DR PathwayCommons; Q8N271; -.
DR SignaLink; Q8N271; -.
DR BioGRID-ORCS; 150696; 10 hits in 1066 CRISPR screens.
DR ChiTaRS; PROM2; human.
DR GenomeRNAi; 150696; -.
DR Pharos; Q8N271; Tbio.
DR PRO; PR:Q8N271; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8N271; protein.
DR Bgee; ENSG00000155066; Expressed in esophagus squamous epithelium and 159 other tissues.
DR ExpressionAtlas; Q8N271; baseline and differential.
DR Genevisible; Q8N271; HS.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:CAFA.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; ISS:CAFA.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:CAFA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:CAFA.
DR GO; GO:0044393; C:microspike; ISS:CAFA.
DR GO; GO:0005902; C:microvillus; ISS:CAFA.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071914; C:prominosome; ISS:CAFA.
DR GO; GO:0015485; F:cholesterol binding; ISS:CAFA.
DR GO; GO:2001287; P:negative regulation of caveolin-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:0048550; P:negative regulation of pinocytosis; IDA:UniProtKB.
DR GO; GO:0031346; P:positive regulation of cell projection organization; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR InterPro; IPR008795; Prominin.
DR PANTHER; PTHR22730; PTHR22730; 1.
DR Pfam; PF05478; Prominin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..834
FT /note="Prominin-2"
FT /id="PRO_0000331239"
FT TOPO_DOM 27..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..779
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 780..800
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 801..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ52"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..474
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033148"
FT VAR_SEQ 576..624
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033149"
FT VARIANT 508
FT /note="Q -> R (in dbSNP:rs12992066)"
FT /evidence="ECO:0000269|PubMed:12514187,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_042749"
FT CONFLICT 340
FT /note="P -> L (in Ref. 3; BAF83055)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="G -> S (in Ref. 3; BAC03657)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="T -> A (in Ref. 3; BAC03657)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="V -> I (in Ref. 3; BAC03657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 91883 MW; 95C4D88AED2806A3 CRC64;
MKHTLALLAP LLGLGLGLAL SQLAAGATDC KFLGPAEHLT FTPAARARWL APRVRAPGLL
DSLYGTVRRF LSVVQLNPFP SELVKALLNE LASVKVNEVV RYEAGYVVCA VIAGLYLLLV
PTAGLCFCCC RCHRRCGGRV KTEHKALACE RAALMVFLLL TTLLLLIGVV CAFVTNQRTH
EQMGPSIEAM PETLLSLWGL VSDVPQELQA VAQQFSLPQE QVSEELDGVG VSIGSAIHTQ
LRSSVYPLLA AVGSLGQVLQ VSVHHLQTLN ATVVELQAGQ QDLEPAIREH RDRLLELLQE
ARCQGDCAGA LSWARTLELG ADFSQVPSVD HVLHQLKGVP EANFSSMVQE ENSTFNALPA
LAAMQTSSVV QELKKAVAQQ PEGVRTLAEG FPGLEAASRW AQALQEVEES SRPYLQEVQR
YETYRWIVGC VLCSVVLFVV LCNLLGLNLG IWGLSARDDP SHPEAKGEAG ARFLMAGVGL
SFLFAAPLIL LVFATFLVGG NVQTLVCQSW ENGELFEFAD TPGNLPPSMN LSQLLGLRKN
ISIHQAYQQC KEGAALWTVL QLNDSYDLEE HLDINQYTNK LRQELQSLKV DTQSLDLLSS
AARRDLEALQ SSGLQRIHYP DFLVQIQRPV VKTSMEQLAQ ELQGLAQAQD NSVLGQRLQE
EAQGLRNLHQ EKVVPQQSLV AKLNLSVRAL ESSAPNLQLE TSDVLANVTY LKGELPAWAA
RILRNVSECF LAREMGYFSQ YVAWVREEVT QRIATCQPLS GALDNSRVIL CDMMADPWNA
FWFCLAWCTF FLIPSIIFAV KTSKYFRPIR KRLSSTSSEE TQLFHIPRVT SLKL
