JAML_HUMAN
ID JAML_HUMAN Reviewed; 394 AA.
AC Q86YT9; B0YIV1; B0YIV2; Q496M1; Q5DTC6; Q7Z499; Q8N9I7; Q8NF70;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Junctional adhesion molecule-like {ECO:0000312|HGNC:HGNC:19084};
DE AltName: Full=Adhesion molecule interacting with CXADR antigen 1;
DE AltName: Full=Dendritic cell-specific protein CREA7-1;
DE Flags: Precursor;
GN Name=JAML {ECO:0000312|HGNC:HGNC:19084}; Synonyms=AMICA1;
GN ORFNames=UNQ722/PRO1387;
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), FUNCTION IN LEUKOCYTE MIGRATION,
RP INDUCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY, MUTAGENESIS OF
RP LYS-54, AND VARIANT ALA-193.
RC TISSUE=Bone marrow;
RX PubMed=12869515; DOI=10.1182/blood-2002-11-3462;
RA Moog-Lutz C., Cave-Riant F., Guibal F.C., Breau M.A., Di Gioia Y.,
RA Couraud P.O., Cayre Y.E., Bourdoulous S., Lutz P.G.;
RT "JAML, a novel protein with characteristics of a junctional adhesion
RT molecule, is induced during differentiation of myeloid leukemia cells.";
RL Blood 102:3371-3378(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ASN-94 AND ALA-193.
RC TISSUE=Dendritic cell;
RA Ahn J.H., Jung H.R., Lee B.-H., Jeon C.J., Bae Y.-S.;
RT "Dendritic cell specific protein Crea7-1.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP ASN-94 AND ALA-193.
RC TISSUE=Cerebellum, and Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 [8]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [9]
RP FUNCTION IN LEUKOCYTE MIGRATION, INTERACTION WITH CXADR, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RX PubMed=15800062; DOI=10.1091/mbc.e05-01-0036;
RA Zen K., Liu Y., McCall I.C., Wu T., Lee W., Babbin B.A., Nusrat A.,
RA Parkos C.A.;
RT "Neutrophil migration across tight junctions is mediated by adhesive
RT interactions between epithelial CAR and a JAM-like protein on
RT neutrophils.";
RL Mol. Biol. Cell 16:2694-2703(2005).
RN [10]
RP FUNCTION IN LEUKOCYTE MIGRATION, HOMODIMERIZATION, MUTAGENESIS OF LYS-54,
RP INTERACTION WITH CXADR, AND TISSUE SPECIFICITY.
RX PubMed=19064666; DOI=10.1083/jcb.200805061;
RA Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S.;
RT "JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis
RT by alpha4beta1 integrin activation.";
RL J. Cell Biol. 183:1159-1173(2008).
RN [11]
RP FUNCTION IN LEUKOCYTE MIGRATION, AND TISSUE SPECIFICITY.
RX PubMed=18948633; DOI=10.1161/atvbaha.108.177717;
RA Guo Y.L., Bai R., Chen C.X., Liu D.Q., Liu Y., Zhang C.Y., Zen K.;
RT "Role of junctional adhesion molecule-like protein in mediating monocyte
RT transendothelial migration.";
RL Arterioscler. Thromb. Vasc. Biol. 29:75-83(2009).
CC -!- FUNCTION: Transmembrane protein of the plasma membrane of leukocytes
CC that control their migration and activation through interaction with
CC CXADR, a plasma membrane receptor found on adjacent epithelial and
CC endothelial cells. The interaction between both receptors mediates the
CC activation of gamma-delta T-cells, a subpopulation of T-cells residing
CC in epithelia and involved in tissue homeostasis and repair. Upon
CC epithelial CXADR-binding, JAML induces downstream cell signaling events
CC in gamma-delta T-cells through PI3-kinase and MAP kinases. It results
CC in proliferation and production of cytokines and growth factors by T-
CC cells that in turn stimulate epithelial tissues repair. It also
CC controls the transmigration of leukocytes within epithelial and
CC endothelial tissues through adhesive interactions with epithelial and
CC endothelial CXADR. {ECO:0000269|PubMed:12869515,
CC ECO:0000269|PubMed:15800062, ECO:0000269|PubMed:18948633,
CC ECO:0000269|PubMed:19064666}.
CC -!- SUBUNIT: Homodimer; active form in leukocyte-endothelial cell adhesion.
CC Interacts (homodimeric form) with CXADR. Interacts (via cytoplasmic
CC domain) with the PI3 kinase; upon CXADR-binding. Interacts with ITGA4
CC and ITGB1; integrin alpha-4/beta-1 may regulate leukocyte to
CC endothelial cells adhesion by controlling JAML homodimerization.
CC {ECO:0000269|PubMed:15800062, ECO:0000269|PubMed:19064666}.
CC -!- INTERACTION:
CC Q86YT9-2; P21145: MAL; NbExp=3; IntAct=EBI-17244059, EBI-3932027;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12869515};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:12869515}. Cell
CC junction {ECO:0000269|PubMed:12869515}. Note=Localized at the plasma
CC membrane and enriched in areas of cell-cell contacts (PubMed:12869515).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86YT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YT9-2; Sequence=VSP_014830;
CC Name=3;
CC IsoId=Q86YT9-3; Sequence=VSP_014831, VSP_014832;
CC Name=4;
CC IsoId=Q86YT9-4; Sequence=VSP_054911;
CC -!- TISSUE SPECIFICITY: Expression is restricted to the hematopoietic
CC tissues with the exception of liver. Expressed in fetal liver, spleen
CC and thymus. Preferentially expressed by mature leukocytes (at protein
CC level). {ECO:0000269|PubMed:12869515, ECO:0000269|PubMed:18948633,
CC ECO:0000269|PubMed:19064666}.
CC -!- INDUCTION: Up-regulated upon retinoic acid, Me2SO and PMA treatment in
CC differentiating myeloid leukemia cells. {ECO:0000269|PubMed:12869515}.
CC -!- DOMAIN: The Ig-like V-type domain 1 mediates interaction with CXADR (By
CC similarity). The Ig-like V-type domain 2 may also play a role in the
CC interaction (PubMed:15800062). {ECO:0000250,
CC ECO:0000269|PubMed:12869515, ECO:0000269|PubMed:15800062}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03390.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ515553; CAD56620.2; -; mRNA.
DR EMBL; AY093686; AAM15730.1; -; mRNA.
DR EMBL; AY138965; AAN52117.1; -; mRNA.
DR EMBL; AY358362; AAQ88728.1; -; mRNA.
DR EMBL; AK090409; BAC03390.1; ALT_INIT; mRNA.
DR EMBL; AK094399; BAC04347.1; -; mRNA.
DR EMBL; EF444945; ACA05929.1; -; Genomic_DNA.
DR EMBL; EF444945; ACA05930.1; -; Genomic_DNA.
DR EMBL; AP002800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100797; AAI00798.1; -; mRNA.
DR CCDS; CCDS41723.1; -. [Q86YT9-1]
DR CCDS; CCDS66240.1; -. [Q86YT9-4]
DR CCDS; CCDS8391.1; -. [Q86YT9-2]
DR RefSeq; NP_001091996.1; NM_001098526.1. [Q86YT9-1]
DR RefSeq; NP_001273499.1; NM_001286570.1. [Q86YT9-4]
DR RefSeq; NP_001273500.1; NM_001286571.1. [Q86YT9-4]
DR RefSeq; NP_694938.2; NM_153206.2. [Q86YT9-2]
DR AlphaFoldDB; Q86YT9; -.
DR SMR; Q86YT9; -.
DR BioGRID; 125686; 2.
DR IntAct; Q86YT9; 5.
DR STRING; 9606.ENSP00000348635; -.
DR GlyGen; Q86YT9; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q86YT9; -.
DR PhosphoSitePlus; Q86YT9; -.
DR SwissPalm; Q86YT9; -.
DR BioMuta; JAML; -.
DR DMDM; 71151910; -.
DR EPD; Q86YT9; -.
DR jPOST; Q86YT9; -.
DR MassIVE; Q86YT9; -.
DR PaxDb; Q86YT9; -.
DR PeptideAtlas; Q86YT9; -.
DR PRIDE; Q86YT9; -.
DR ProteomicsDB; 61996; -.
DR ProteomicsDB; 70469; -. [Q86YT9-1]
DR ProteomicsDB; 70470; -. [Q86YT9-2]
DR ProteomicsDB; 70471; -. [Q86YT9-3]
DR Antibodypedia; 32431; 287 antibodies from 27 providers.
DR DNASU; 120425; -.
DR Ensembl; ENST00000292067.11; ENSP00000292067.7; ENSG00000160593.19. [Q86YT9-2]
DR Ensembl; ENST00000356289.10; ENSP00000348635.5; ENSG00000160593.19. [Q86YT9-1]
DR Ensembl; ENST00000526620.5; ENSP00000431218.1; ENSG00000160593.19. [Q86YT9-4]
DR GeneID; 120425; -.
DR KEGG; hsa:120425; -.
DR MANE-Select; ENST00000356289.10; ENSP00000348635.5; NM_001098526.2; NP_001091996.1.
DR UCSC; uc001psi.3; human. [Q86YT9-1]
DR CTD; 120425; -.
DR DisGeNET; 120425; -.
DR GeneCards; JAML; -.
DR HGNC; HGNC:19084; JAML.
DR HPA; ENSG00000160593; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 609770; gene.
DR neXtProt; NX_Q86YT9; -.
DR OpenTargets; ENSG00000160593; -.
DR PharmGKB; PA38792; -.
DR VEuPathDB; HostDB:ENSG00000160593; -.
DR eggNOG; ENOG502SVGE; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR InParanoid; Q86YT9; -.
DR OMA; PVWPSLK; -.
DR OrthoDB; 1154501at2759; -.
DR PhylomeDB; Q86YT9; -.
DR TreeFam; TF331728; -.
DR PathwayCommons; Q86YT9; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; Q86YT9; -.
DR BioGRID-ORCS; 120425; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; JAML; human.
DR GeneWiki; AMICA1; -.
DR GenomeRNAi; 120425; -.
DR Pharos; Q86YT9; Tbio.
DR PRO; PR:Q86YT9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86YT9; protein.
DR Bgee; ENSG00000160593; Expressed in monocyte and 155 other tissues.
DR ExpressionAtlas; Q86YT9; baseline and differential.
DR Genevisible; Q86YT9; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0046629; P:gamma-delta T cell activation; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR GO; GO:0035696; P:monocyte extravasation; IMP:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:UniProtKB.
DR GO; GO:0072672; P:neutrophil extravasation; IMP:UniProtKB.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR029871; JAML.
DR InterPro; IPR000920; Myelin_P0-rel.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF22; PTHR13869:SF22; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 20..394
FT /note="Junctional adhesion molecule-like"
FT /id="PRO_0000015074"
FT TOPO_DOM 20..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..132
FT /note="Ig-like V-type 1"
FT DOMAIN 137..250
FT /note="Ig-like V-type 2"
FT REGION 369..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054911"
FT VAR_SEQ 1..14
FT /note="MFCPLKLILLPVLL -> MVSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014830"
FT VAR_SEQ 258..259
FT /note="TL -> SI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014831"
FT VAR_SEQ 260..394
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014832"
FT VARIANT 94
FT /note="I -> N (in dbSNP:rs17121881)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_049974"
FT VARIANT 193
FT /note="V -> A (in dbSNP:rs1793174)"
FT /evidence="ECO:0000269|PubMed:12869515,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_049975"
FT VARIANT 322
FT /note="I -> M (in dbSNP:rs2298831)"
FT /id="VAR_049976"
FT MUTAGEN 54
FT /note="K->E: Loss of the ability to homodimerize, loss of
FT interaction with CXADR and loss of function in cell-cell
FT adhesion."
FT /evidence="ECO:0000269|PubMed:12869515,
FT ECO:0000269|PubMed:19064666"
FT CONFLICT 283
FT /note="C -> G (in Ref. 2; AAM15730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 44339 MW; 64B542F9384C7642 CRC64;
MFCPLKLILL PVLLDYSLGL NDLNVSPPEL TVHVGDSALM GCVFQSTEDK CIFKIDWTLS
PGEHAKDEYV LYYYSNLSVP IGRFQNRVHL MGDILCNDGS LLLQDVQEAD QGTYICEIRL
KGESQVFKKA VVLHVLPEEP KELMVHVGGL IQMGCVFQST EVKHVTKVEW IFSGRRAKEE
IVFRYYHKLR MSVEYSQSWG HFQNRVNLVG DIFRNDGSIM LQGVRESDGG NYTCSIHLGN
LVFKKTIVLH VSPEEPRTLV TPAALRPLVL GGNQLVIIVG IVCATILLLP VLILIVKKTC
GNKSSVNSTV LVKNTKKTNP EIKEKPCHFE RCEGEKHIYS PIIVREVIEE EEPSEKSEAT
YMTMHPVWPS LRSDRNNSLE KKSGGGMPKT QQAF
