JAM1_MOUSE
ID JAM1_MOUSE Reviewed; 300 AA.
AC O88792; Q8VC39;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Junctional adhesion molecule A;
DE Short=JAM-A;
DE AltName: Full=Junctional adhesion molecule 1;
DE Short=JAM-1;
DE AltName: CD_antigen=CD321;
DE Flags: Precursor;
GN Name=F11r; Synonyms=Jam1, Jcam, Jcam1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9660867; DOI=10.1083/jcb.142.1.117;
RA Martin-Padura I., Lostaglio S., Schneemann M., Williams L., Romano M.,
RA Fruscella P., Panzeri C., Stoppacciaro A., Ruco L., Villa A., Simmons D.,
RA Dejana E.;
RT "Junctional adhesion molecule, a novel member of the immunoglobulin
RT superfamily that distributes at intercellular junctions and modulates
RT monocyte transmigration.";
RL J. Cell Biol. 142:117-127(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11036763; DOI=10.1007/978-3-642-57276-0_12;
RA Aurrand-Lions M.A., Duncan L., Du Pasquier L., Imhof B.A.;
RT "Cloning of JAM-2 and JAM-3: an emerging junctional adhesion molecular
RT family?";
RL Curr. Top. Microbiol. Immunol. 251:91-98(2000).
RN [7]
RP INTERACTION WITH PARD3.
RX PubMed=11447115; DOI=10.1093/emboj/20.14.3738;
RA Ebnet K., Suzuki A., Horikoshi Y., Hirose T., Meyer zu Brickwedde M.-K.,
RA Ohno S., Vestweber D.;
RT "The cell polarity protein ASIP/PAR-3 directly associates with junctional
RT adhesion molecule (JAM).";
RL EMBO J. 20:3738-3748(2001).
RN [8]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=12810109; DOI=10.1016/s1471-4906(03)00117-0;
RA Muller W.A.;
RT "Leukocyte-endothelial-cell interactions in leukocyte transmigration and
RT the inflammatory response.";
RL Trends Immunol. 24:327-334(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42 AND ASN-185.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 27-238, AND DISULFIDE BONDS.
RX PubMed=11500366; DOI=10.1093/emboj/20.16.4391;
RA Kostrewa D., Brockhaus M., D'Arcy A., Dale G.E., Nelboeck P., Schmid G.,
RA Mueller F., Bazzoni G., Dejana E., Bartfai T., Winkler F.K., Hennig M.;
RT "X-ray structure of junctional adhesion molecule: structural basis for
RT homophilic adhesion via a novel dimerization motif.";
RL EMBO J. 20:4391-4398(2001).
CC -!- FUNCTION: Seems to play a role in epithelial tight junction formation.
CC Appears early in primordial forms of cell junctions and recruits PARD3
CC (PubMed:11447115). The association of the PARD6-PARD3 complex may
CC prevent the interaction of PARD3 with JAM1, thereby preventing tight
CC junction assembly (PubMed:11447115). Plays a role in regulating
CC monocyte transmigration involved in integrity of epithelial barrier
CC (PubMed:9660867). Ligand for integrin alpha-L/beta-2 involved in memory
CC T-cell and neutrophil transmigration (By similarity). Involved in
CC platelet activation (By similarity). {ECO:0000250|UniProtKB:Q9Y624,
CC ECO:0000269|PubMed:11447115, ECO:0000269|PubMed:9660867}.
CC -!- SUBUNIT: Interacts with the ninth PDZ domain of MPDZ (By similarity).
CC Interacts with the first PDZ domain of PARD3 (PubMed:11447115). The
CC association between PARD3 and PARD6B probably disrupts this interaction
CC (PubMed:11447115). Interacts with ITGAL (via I-domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y624, ECO:0000269|PubMed:11447115}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:11036763}. Cell membrane
CC {ECO:0000269|PubMed:11036763}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11036763}. Note=Localized at tight junctions of
CC both epithelial and endothelial cells.
CC -!- DOMAIN: The Ig-like V-type 2 domain is necessary and sufficient for
CC interaction with integrin alpha-L/beta-2.
CC {ECO:0000250|UniProtKB:Q9Y624}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {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; U89915; AAC32982.1; -; mRNA.
DR EMBL; AK033574; BAC28369.1; -; mRNA.
DR EMBL; CT010347; CAJ18555.1; -; mRNA.
DR EMBL; AC087229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021876; AAH21876.1; -; mRNA.
DR CCDS; CCDS15496.1; -.
DR RefSeq; NP_766235.1; NM_172647.2.
DR PDB; 1F97; X-ray; 2.50 A; A=27-238.
DR PDBsum; 1F97; -.
DR AlphaFoldDB; O88792; -.
DR SMR; O88792; -.
DR BioGRID; 200861; 2.
DR DIP; DIP-41166N; -.
DR IntAct; O88792; 3.
DR MINT; O88792; -.
DR STRING; 10090.ENSMUSP00000041907; -.
DR GlyGen; O88792; 2 sites.
DR iPTMnet; O88792; -.
DR PhosphoSitePlus; O88792; -.
DR EPD; O88792; -.
DR jPOST; O88792; -.
DR PaxDb; O88792; -.
DR PeptideAtlas; O88792; -.
DR PRIDE; O88792; -.
DR ProteomicsDB; 269026; -.
DR ABCD; O88792; 32 sequenced antibodies.
DR Antibodypedia; 3317; 633 antibodies from 44 providers.
DR DNASU; 16456; -.
DR Ensembl; ENSMUST00000043839; ENSMUSP00000041907; ENSMUSG00000038235.
DR GeneID; 16456; -.
DR KEGG; mmu:16456; -.
DR UCSC; uc007doo.1; mouse.
DR CTD; 50848; -.
DR MGI; MGI:1321398; F11r.
DR VEuPathDB; HostDB:ENSMUSG00000038235; -.
DR eggNOG; ENOG502QWVN; Eukaryota.
DR GeneTree; ENSGT00940000159186; -.
DR HOGENOM; CLU_067351_0_0_1; -.
DR InParanoid; O88792; -.
DR OMA; YSRGYFE; -.
DR OrthoDB; 1122085at2759; -.
DR PhylomeDB; O88792; -.
DR TreeFam; TF331459; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-MMU-420029; Tight junction interactions.
DR BioGRID-ORCS; 16456; 4 hits in 72 CRISPR screens.
DR ChiTaRS; F11r; mouse.
DR EvolutionaryTrace; O88792; -.
DR PRO; PR:O88792; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O88792; protein.
DR Bgee; ENSMUSG00000038235; Expressed in saccule of membranous labyrinth and 228 other tissues.
DR Genevisible; O88792; MM.
DR GO; GO:0005923; C:bicellular tight junction; IMP:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0036057; C:slit diaphragm; ISO:MGI.
DR GO; GO:0070160; C:tight junction; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:MGI.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:MGI.
DR GO; GO:0050892; P:intestinal absorption; IMP:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0035683; P:memory T cell extravasation; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISO:MGI.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; ISO:MGI.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IMP:CACAO.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:MGI.
DR GO; GO:0090559; P:regulation of membrane permeability; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042456; F11R.
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; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR45113; PTHR45113; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..300
FT /note="Junctional adhesion molecule A"
FT /id="PRO_0000015067"
FT TOPO_DOM 27..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..122
FT /note="Ig-like V-type 1"
FT DOMAIN 134..230
FT /note="Ig-like V-type 2"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y624"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT DISULFID 49..108
FT /evidence="ECO:0000269|PubMed:11500366,
FT ECO:0007744|PDB:1F97"
FT DISULFID 152..212
FT /evidence="ECO:0000269|PubMed:11500366,
FT ECO:0007744|PDB:1F97"
FT CONFLICT 268
FT /note="R -> T (in Ref. 1; AAC32982)"
FT /evidence="ECO:0000305"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1F97"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1F97"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1F97"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 115..129
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1F97"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1F97"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1F97"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:1F97"
SQ SEQUENCE 300 AA; 32424 MW; 3CE561E8FF3B97EC CRC64;
MGTEGKAGRK LLFLFTSMIL GSLVQGKGSV YTAQSDVQVP ENESIKLTCT YSGFSSPRVE
WKFVQGSTTA LVCYNSQITA PYADRVTFSS SGITFSSVTR KDNGEYTCMV SEEGGQNYGE
VSIHLTVLVP PSKPTISVPS SVTIGNRAVL TCSEHDGSPP SEYSWFKDGI SMLTADAKKT
RAFMNSSFTI DPKSGDLIFD PVTAFDSGEY YCQAQNGYGT AMRSEAAHMD AVELNVGGIV
AAVLVTLILL GLLIFGVWFA YSRGYFERTK KGTAPGKKVI YSQPSTRSEG EFKQTSSFLV
