CD44_MOUSE
ID CD44_MOUSE Reviewed; 778 AA.
AC P15379; Q05732; Q61395; Q62060; Q62061; Q62062; Q62063; Q62408; Q62409;
AC Q64296; Q99J14; Q9QYX8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=CD44 antigen;
DE AltName: Full=Extracellular matrix receptor III;
DE Short=ECMR-III;
DE AltName: Full=GP90 lymphocyte homing/adhesion receptor;
DE AltName: Full=HUTCH-I;
DE AltName: Full=Hermes antigen;
DE AltName: Full=Hyaluronate receptor;
DE AltName: Full=Lymphocyte antigen 24;
DE Short=Ly-24;
DE AltName: Full=Phagocytic glycoprotein 1;
DE Short=PGP-1;
DE AltName: Full=Phagocytic glycoprotein I;
DE Short=PGP-I;
DE AltName: CD_antigen=CD44;
DE Flags: Precursor;
GN Name=Cd44; Synonyms=Ly-24;
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] (ISOFORMS 4; 6; 7 AND 12).
RC STRAIN=DBA/2J; TISSUE=Lung;
RX PubMed=1469058; DOI=10.1083/jcb.119.6.1711;
RA He Q., Lesley J., Hyman R., Ishihara K., Kincade P.W.;
RT "Molecular isoforms of murine CD44 and evidence that the membrane proximal
RT domain is not critical for hyaluronate recognition.";
RL J. Cell Biol. 119:1711-1719(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13), AND POLYMORPHISM.
RX PubMed=2681416;
RA Zhou D.F.H., Ding J.F., Picker L.J., Bargatze R.F., Butcher E.C.,
RA Goeddel D.V.;
RT "Molecular cloning and expression of Pgp-1. The mouse homolog of the human
RT H-CAM (Hermes) lymphocyte homing receptor.";
RL J. Immunol. 143:3390-3395(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
RX PubMed=2682651; DOI=10.1073/pnas.86.21.8521;
RA Nottenburg C., Rees G., St John T.;
RT "Isolation of mouse CD44 cDNA: structural features are distinct from the
RT primate cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8521-8525(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=10859330; DOI=10.1084/jem.191.12.2053;
RA Wittig B.M., Johansson B., Zoeller M., Schwaerzler C., Guenthert U.;
RT "Abrogation of experimental colitis correlates with increased apoptosis in
RT mice deficient for CD44 variant exon 7 (CD44v7).";
RL J. Exp. Med. 191:2053-2064(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-778 (ISOFORM 13).
RX PubMed=2403559; DOI=10.1016/s0021-9258(19)40235-4;
RA Wolffe E.J., Gause W.C., Pelfrey C.M., Holland S.M., Steinberg A.D.,
RA August J.T.;
RT "The cDNA sequence of mouse Pgp-1 and homology to human CD44 cell surface
RT antigen and proteoglycan core/link proteins.";
RL J. Biol. Chem. 265:341-347(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8).
RC STRAIN=GR;
RX PubMed=8464707; DOI=10.1093/nar/21.5.1225;
RA Toelg C., Hofmann M., Herrlich P., Ponta H.;
RT "Splicing choice from ten variant exons establishes CD44 variability.";
RL Nucleic Acids Res. 21:1225-1229(1993).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORM 9).
RC STRAIN=BALB/cJ;
RX PubMed=8509359; DOI=10.1016/s0021-9258(18)31376-0;
RA Screaton G.R., Bell M.V., Bell J.I., Jackson D.G.;
RT "The identification of a new alternative exon with highly restricted tissue
RT expression in transcripts encoding the mouse Pgp-1 (CD44) homing receptor.
RT Comparison of all 10 variable exons between mouse, human, and rat.";
RL J. Biol. Chem. 268:12235-12238(1993).
RN [10]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 10 AND 11).
RC STRAIN=Swiss Webster;
RX PubMed=8702806; DOI=10.1074/jbc.271.34.20603;
RA Yu Q., Toole B.P.;
RT "A new alternatively spliced exon between v9 and v10 provides a molecular
RT basis for synthesis of soluble CD44.";
RL J. Biol. Chem. 271:20603-20607(1996).
RN [11]
RP FUNCTION, AND INTERACTION WITH CD74.
RX PubMed=8343954; DOI=10.1016/0092-8674(93)90417-o;
RA Naujokas M.F., Morin M., Anderson M.S., Peterson M., Miller J.;
RT "The chondroitin sulfate form of invariant chain can enhance stimulation of
RT T cell responses through interaction with CD44.";
RL Cell 74:257-268(1993).
RN [12]
RP INTERACTION WITH EZR; MSN AND RDX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 715-LYS--LYS-717.
RX PubMed=9472040; DOI=10.1083/jcb.140.4.885;
RA Yonemura S., Hirao M., Doi Y., Takahashi N., Kondo T., Tsukita S.,
RA Tsukita S.;
RT "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino
RT acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and
RT ICAM-2.";
RL J. Cell Biol. 140:885-895(1998).
RN [13]
RP INTERACTION WITH PKN2, AND SUBCELLULAR LOCATION.
RX PubMed=17403031; DOI=10.1111/j.1471-4159.2007.04485.x;
RA Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.;
RT "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase
RT activation leading to cytoskeleton function and cell migration in
RT astrocytes.";
RL J. Neurochem. 101:1002-1017(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726; SER-733 AND SER-742, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726 AND SER-742, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
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 [16]
RP INTERACTION WITH TIAM1 AND TIAM2.
RX PubMed=19893486; DOI=10.1038/emboj.2009.323;
RA Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T.,
RA Kaibuchi K., Hakoshima T.;
RT "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding
RT module.";
RL EMBO J. 29:236-250(2010).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25065622; DOI=10.1016/j.immuni.2014.06.011;
RA Wu C., Thalhamer T., Franca R.F., Xiao S., Wang C., Hotta C., Zhu C.,
RA Hirashima M., Anderson A.C., Kuchroo V.K.;
RT "Galectin-9-CD44 interaction enhances stability and function of adaptive
RT regulatory T cells.";
RL Immunity 41:270-282(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 23-174 ALONE AND IN COMPLEX WITH
RP HYALURONAN, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=17293874; DOI=10.1038/nsmb1201;
RA Banerji S., Wright A.J., Noble M., Mahoney D.J., Campbell I.D., Day A.J.,
RA Jackson D.G.;
RT "Structures of the Cd44-hyaluronan complex provide insight into a
RT fundamental carbohydrate-protein interaction.";
RL Nat. Struct. Mol. Biol. 14:234-239(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 708-727, INTERACTION WITH RDX,
RP AND DISULFIDE BOND.
RX PubMed=18753140; DOI=10.1074/jbc.m803606200;
RA Mori T., Kitano K., Terawaki S., Maesaki R., Fukami Y., Hakoshima T.;
RT "Structural basis for CD44 recognition by ERM proteins.";
RL J. Biol. Chem. 283:29602-29612(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 23-171, INTERACTION WITH HA, AND
RP DISULFIDE BOND.
RX PubMed=24606063; DOI=10.1021/jm5000276;
RA Liu L.K., Finzel B.C.;
RT "Fragment-based identification of an inducible binding site on cell surface
RT receptor CD44 for the design of protein-carbohydrate interaction
RT inhibitors.";
RL J. Med. Chem. 57:2714-2725(2014).
CC -!- FUNCTION: Cell-surface receptor that plays a role in cell-cell
CC interactions, cell adhesion and migration, helping them to sense and
CC respond to changes in the tissue microenvironment. Participates thereby
CC in a wide variety of cellular functions including the activation,
CC recirculation and homing of T-lymphocytes, hematopoiesis, inflammation
CC and response to bacterial infection. Engages, through its ectodomain,
CC extracellular matrix components such as hyaluronan/HA, collagen, growth
CC factors, cytokines or proteases and serves as a platform for signal
CC transduction by assembling, via its cytoplasmic domain, protein
CC complexes containing receptor kinases and membrane proteases
CC (PubMed:8343954, PubMed:25065622). Such effectors include PKN2, the
CC RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that
CC coordinate signaling pathways promoting calcium mobilization and actin-
CC mediated cytoskeleton reorganization essential for cell migration and
CC adhesion (By similarity). {ECO:0000250|UniProtKB:P16070,
CC ECO:0000269|PubMed:25065622, ECO:0000269|PubMed:8343954}.
CC -!- SUBUNIT: Interacts with PKN2 (PubMed:17403031). Interacts with TIAM1
CC and TIAM2 (PubMed:19893486). Interacts with HA, as well as other
CC glycosaminoglycans, collagen, laminin, and fibronectin via its N-
CC terminal segment (PubMed:24606063). Interacts with UNC119. Interacts
CC with PDPN (via extracellular domain); this interaction is required for
CC PDPN-mediated directional migration and regulation of lamellipodia
CC extension/stabilization during cell spreading and migration (By
CC similarity). Interacts with RDX, EZR and MSN (via FERM domain)
CC (PubMed:9472040, PubMed:18753140). Interacts with EGFR (By similarity).
CC Interacts with CD74; this complex is essential for the MIF-induced
CC signaling cascade that results in B cell survival (PubMed:8343954).
CC {ECO:0000250|UniProtKB:P16070, ECO:0000269|PubMed:17403031,
CC ECO:0000269|PubMed:18753140, ECO:0000269|PubMed:19893486,
CC ECO:0000269|PubMed:24606063, ECO:0000269|PubMed:8343954,
CC ECO:0000269|PubMed:9472040}.
CC -!- INTERACTION:
CC P15379; O08573: Lgals9; NbExp=2; IntAct=EBI-7565891, EBI-8377586;
CC P15379; Q64729: Tgfbr1; NbExp=4; IntAct=EBI-7565891, EBI-2899393;
CC P15379; Q60610: Tiam1; NbExp=8; IntAct=EBI-7565891, EBI-1030321;
CC P15379; Q6ZPF3: Tiam2; NbExp=8; IntAct=EBI-7565891, EBI-7565978;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17403031,
CC ECO:0000269|PubMed:25065622}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:17403031}. Cell projection, microvillus
CC {ECO:0000269|PubMed:9472040}. Note=Colocalizes with actin in membrane
CC protrusionFs at wounding edges. Co-localizes with RDX, EZR and MSN in
CC microvilli. {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:9472040}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Name=1;
CC IsoId=P15379-14; Sequence=Displayed;
CC Name=2;
CC IsoId=P15379-7; Sequence=VSP_007329;
CC Name=3;
CC IsoId=P15379-8; Sequence=VSP_007330;
CC Name=4; Synonyms=M2;
CC IsoId=P15379-4; Sequence=VSP_007331;
CC Name=5;
CC IsoId=P15379-9; Sequence=VSP_007332;
CC Name=6; Synonyms=M3;
CC IsoId=P15379-5; Sequence=VSP_005326;
CC Name=7; Synonyms=M4;
CC IsoId=P15379-6; Sequence=VSP_005327;
CC Name=8;
CC IsoId=P15379-10; Sequence=VSP_007330, VSP_007334;
CC Name=9;
CC IsoId=P15379-11; Sequence=VSP_007332, VSP_007335;
CC Name=10;
CC IsoId=P15379-12; Sequence=VSP_007336, VSP_007337;
CC Name=11;
CC IsoId=P15379-13; Sequence=VSP_007338, VSP_007339;
CC Name=12; Synonyms=M1;
CC IsoId=P15379-3; Sequence=VSP_005328;
CC Name=13; Synonyms=M0;
CC IsoId=P15379-2; Sequence=VSP_005329, VSP_007333;
CC -!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan
CC binding.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P16070}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate glycans which can be
CC more or less sulfated. {ECO:0000250|UniProtKB:P16070}.
CC -!- PTM: Phosphorylated; activation of PKC results in the dephosphorylation
CC of Ser-742 (constitutive phosphorylation site), and the phosphorylation
CC of Ser-708. {ECO:0000250}.
CC -!- POLYMORPHISM: Two allelic forms of this glycoprotein, PGP-1.1 and PGP-
CC 1.2, have been reported. The expressed product is PGP-1.1 (Ly-24.1).
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DR EMBL; X66084; CAA46883.1; -; mRNA.
DR EMBL; X66083; CAA46882.1; -; mRNA.
DR EMBL; X66082; CAA46881.1; -; mRNA.
DR EMBL; X66081; CAA46880.1; -; mRNA.
DR EMBL; M30655; AAA39922.1; -; mRNA.
DR EMBL; M27129; AAA37406.1; -; mRNA.
DR EMBL; M27130; AAA37407.1; -; mRNA.
DR EMBL; AJ251594; CAB61888.1; -; mRNA.
DR EMBL; BC005676; AAH05676.1; -; mRNA.
DR EMBL; AK045226; BAC32269.1; -; mRNA.
DR EMBL; J05163; AAA39923.1; -; mRNA.
DR EMBL; X69724; CAA49380.1; -; mRNA.
DR EMBL; L13611; AAA37145.1; -; mRNA.
DR EMBL; U57610; AAC52804.1; -; mRNA.
DR EMBL; U57611; AAB08756.1; -; mRNA.
DR EMBL; U57612; AAC52805.1; -; Genomic_DNA.
DR EMBL; U57612; AAC52806.1; -; Genomic_DNA.
DR PIR; A34424; A34424.
DR PIR; A37009; A37009.
DR PIR; B44355; B44355.
DR PIR; D44355; D44355.
DR PIR; S30397; S30397.
DR RefSeq; NP_001034240.1; NM_001039151.1.
DR RefSeq; NP_001171256.1; NM_001177785.1.
DR RefSeq; NP_001171257.1; NM_001177786.1.
DR RefSeq; NP_001171258.1; NM_001177787.1.
DR RefSeq; NP_033981.2; NM_009851.2.
DR PDB; 2JCP; X-ray; 1.30 A; A=23-174.
DR PDB; 2JCQ; X-ray; 1.25 A; A=23-174.
DR PDB; 2JCR; X-ray; 2.00 A; A=23-174.
DR PDB; 2ZPY; X-ray; 2.10 A; B=708-727.
DR PDB; 4MRD; X-ray; 2.55 A; A=23-171.
DR PDB; 4MRE; X-ray; 1.58 A; A=23-171.
DR PDB; 4MRF; X-ray; 1.55 A; A=23-171.
DR PDB; 4MRG; X-ray; 1.69 A; A=23-171.
DR PDB; 4MRH; X-ray; 1.12 A; A=23-171.
DR PDB; 4NP2; X-ray; 1.75 A; A=23-171.
DR PDB; 4NP3; X-ray; 1.61 A; A=23-171.
DR PDB; 5BZC; X-ray; 1.95 A; A=22-171.
DR PDB; 5BZE; X-ray; 1.31 A; A=23-171.
DR PDB; 5BZF; X-ray; 2.77 A; A=21-171.
DR PDB; 5BZG; X-ray; 2.19 A; A=21-171.
DR PDB; 5BZH; X-ray; 1.95 A; A=21-171.
DR PDB; 5BZI; X-ray; 1.32 A; A=21-171.
DR PDB; 5BZJ; X-ray; 1.40 A; A=21-171.
DR PDB; 5BZK; X-ray; 1.40 A; A=21-171.
DR PDB; 5BZL; X-ray; 1.23 A; A=21-171.
DR PDB; 5BZM; X-ray; 1.25 A; A=21-171.
DR PDB; 5BZN; X-ray; 1.23 A; A=21-171.
DR PDB; 5BZO; X-ray; 1.22 A; A=21-171.
DR PDB; 5BZP; X-ray; 1.23 A; A=21-171.
DR PDB; 5BZQ; X-ray; 1.20 A; A=21-171.
DR PDB; 5BZR; X-ray; 1.15 A; A=21-171.
DR PDB; 5BZS; X-ray; 1.50 A; A=21-171.
DR PDB; 5BZT; X-ray; 1.25 A; A=21-171.
DR PDB; 5SBK; X-ray; 1.23 A; A=23-172.
DR PDB; 5SBL; X-ray; 1.20 A; A=23-172.
DR PDB; 5SBM; X-ray; 1.14 A; A=23-172.
DR PDB; 5SBN; X-ray; 1.18 A; A=23-172.
DR PDB; 5SBO; X-ray; 1.27 A; A=23-172.
DR PDB; 5SBP; X-ray; 1.27 A; A=23-172.
DR PDB; 5SBQ; X-ray; 0.99 A; A=23-172.
DR PDB; 5SBR; X-ray; 1.29 A; A=23-172.
DR PDB; 5SBS; X-ray; 1.02 A; A=23-172.
DR PDB; 5SBT; X-ray; 1.16 A; A=23-172.
DR PDB; 5SBU; X-ray; 1.04 A; A=23-172.
DR PDB; 5SBV; X-ray; 1.11 A; A=23-172.
DR PDB; 5SBW; X-ray; 1.15 A; A=23-172.
DR PDB; 5SBX; X-ray; 1.05 A; A=23-172.
DR PDB; 5SBY; X-ray; 1.22 A; A=23-172.
DR PDB; 5SBZ; X-ray; 1.17 A; A=23-172.
DR PDB; 5SC0; X-ray; 1.19 A; A=23-172.
DR PDB; 5SC1; X-ray; 1.17 A; A=23-172.
DR PDB; 5SC2; X-ray; 1.21 A; A=23-172.
DR PDB; 5SC3; X-ray; 1.24 A; A=23-172.
DR PDB; 5SC4; X-ray; 1.17 A; A=23-172.
DR PDB; 5SC5; X-ray; 1.17 A; A=23-172.
DR PDB; 5SC6; X-ray; 1.33 A; A=23-172.
DR PDB; 5SC7; X-ray; 1.20 A; A=23-172.
DR PDBsum; 2JCP; -.
DR PDBsum; 2JCQ; -.
DR PDBsum; 2JCR; -.
DR PDBsum; 2ZPY; -.
DR PDBsum; 4MRD; -.
DR PDBsum; 4MRE; -.
DR PDBsum; 4MRF; -.
DR PDBsum; 4MRG; -.
DR PDBsum; 4MRH; -.
DR PDBsum; 4NP2; -.
DR PDBsum; 4NP3; -.
DR PDBsum; 5BZC; -.
DR PDBsum; 5BZE; -.
DR PDBsum; 5BZF; -.
DR PDBsum; 5BZG; -.
DR PDBsum; 5BZH; -.
DR PDBsum; 5BZI; -.
DR PDBsum; 5BZJ; -.
DR PDBsum; 5BZK; -.
DR PDBsum; 5BZL; -.
DR PDBsum; 5BZM; -.
DR PDBsum; 5BZN; -.
DR PDBsum; 5BZO; -.
DR PDBsum; 5BZP; -.
DR PDBsum; 5BZQ; -.
DR PDBsum; 5BZR; -.
DR PDBsum; 5BZS; -.
DR PDBsum; 5BZT; -.
DR PDBsum; 5SBK; -.
DR PDBsum; 5SBL; -.
DR PDBsum; 5SBM; -.
DR PDBsum; 5SBN; -.
DR PDBsum; 5SBO; -.
DR PDBsum; 5SBP; -.
DR PDBsum; 5SBQ; -.
DR PDBsum; 5SBR; -.
DR PDBsum; 5SBS; -.
DR PDBsum; 5SBT; -.
DR PDBsum; 5SBU; -.
DR PDBsum; 5SBV; -.
DR PDBsum; 5SBW; -.
DR PDBsum; 5SBX; -.
DR PDBsum; 5SBY; -.
DR PDBsum; 5SBZ; -.
DR PDBsum; 5SC0; -.
DR PDBsum; 5SC1; -.
DR PDBsum; 5SC2; -.
DR PDBsum; 5SC3; -.
DR PDBsum; 5SC4; -.
DR PDBsum; 5SC5; -.
DR PDBsum; 5SC6; -.
DR PDBsum; 5SC7; -.
DR AlphaFoldDB; P15379; -.
DR SMR; P15379; -.
DR BioGRID; 198600; 3.
DR CORUM; P15379; -.
DR DIP; DIP-29095N; -.
DR IntAct; P15379; 14.
DR MINT; P15379; -.
DR STRING; 10090.ENSMUSP00000005218; -.
DR BindingDB; P15379; -.
DR ChEMBL; CHEMBL3232693; -.
DR GlyGen; P15379; 10 sites.
DR iPTMnet; P15379; -.
DR PhosphoSitePlus; P15379; -.
DR SwissPalm; P15379; -.
DR EPD; P15379; -.
DR jPOST; P15379; -.
DR MaxQB; P15379; -.
DR PaxDb; P15379; -.
DR PeptideAtlas; P15379; -.
DR PRIDE; P15379; -.
DR ProteomicsDB; 279969; -. [P15379-14]
DR ProteomicsDB; 279970; -. [P15379-7]
DR ProteomicsDB; 279971; -. [P15379-8]
DR ProteomicsDB; 279972; -. [P15379-4]
DR ProteomicsDB; 279973; -. [P15379-9]
DR ProteomicsDB; 279974; -. [P15379-5]
DR ProteomicsDB; 279975; -. [P15379-6]
DR ProteomicsDB; 279976; -. [P15379-10]
DR ProteomicsDB; 279977; -. [P15379-11]
DR ProteomicsDB; 279978; -. [P15379-12]
DR ProteomicsDB; 279979; -. [P15379-13]
DR ProteomicsDB; 279980; -. [P15379-3]
DR ProteomicsDB; 279981; -. [P15379-2]
DR DNASU; 12505; -.
DR GeneID; 12505; -.
DR KEGG; mmu:12505; -.
DR CTD; 960; -.
DR MGI; MGI:88338; Cd44.
DR eggNOG; ENOG502RX7Q; Eukaryota.
DR InParanoid; P15379; -.
DR OrthoDB; 1098342at2759; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
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-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 12505; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Cd44; mouse.
DR EvolutionaryTrace; P15379; -.
DR PRO; PR:P15379; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P15379; protein.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0042995; C:cell projection; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0005540; F:hyaluronic acid binding; IMP:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IPI:UniProtKB.
DR GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:MGI.
DR GO; GO:0030214; P:hyaluronan catabolic process; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0034238; P:macrophage fusion; ISO:MGI.
DR GO; GO:0070487; P:monocyte aggregation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IMP:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IDA:BHF-UCL.
DR GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; NAS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:1900625; P:positive regulation of monocyte aggregation; ISO:MGI.
DR GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; ISS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR GO; GO:0002246; P:wound healing involved in inflammatory response; IMP:MGI.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
DR Gene3D; 3.10.100.10; -; 1.
DR IDEAL; IID50199; -.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR001231; CD44_antigen.
DR InterPro; IPR043210; CD44_antigen-like.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR10225; PTHR10225; 2.
DR PANTHER; PTHR10225:SF6; PTHR10225:SF6; 2.
DR Pfam; PF00193; Xlink; 1.
DR PRINTS; PR00658; CD44.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Proteoglycan; Receptor; Reference proteome; Signal; Sulfation;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..778
FT /note="CD44 antigen"
FT /id="PRO_0000026689"
FT TOPO_DOM 23..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..123
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT REGION 227..685
FT /note="Stem"
FT REGION 251..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..727
FT /note="Required for interaction with EZR, MSN and RDX and
FT for the co-localization to microvilli"
FT /evidence="ECO:0000269|PubMed:9472040"
FT COMPBIAS 293..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000269|PubMed:17293874"
FT BINDING 80
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000269|PubMed:17293874"
FT BINDING 81
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000269|PubMed:17293874"
FT BINDING 107
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000269|PubMed:17293874"
FT MOD_RES 410
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 708
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P16070"
FT MOD_RES 726
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323,
FT ECO:0000269|PubMed:17293874, ECO:0000269|PubMed:18753140,
FT ECO:0000269|PubMed:24606063"
FT DISULFID 55..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323,
FT ECO:0000269|PubMed:17293874, ECO:0000269|PubMed:18753140,
FT ECO:0000269|PubMed:24606063"
FT DISULFID 79..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323,
FT ECO:0000269|PubMed:17293874, ECO:0000269|PubMed:18753140,
FT ECO:0000269|PubMed:24606063"
FT VAR_SEQ 223..637
FT /note="Missing (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:2403559,
FT ECO:0000303|PubMed:2681416, ECO:0000303|PubMed:2682651"
FT /id="VSP_005329"
FT VAR_SEQ 223..539
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:1469058"
FT /id="VSP_005328"
FT VAR_SEQ 223..504
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:1469058,
FT ECO:0000303|PubMed:8464707"
FT /id="VSP_005327"
FT VAR_SEQ 223..424
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:1469058,
FT ECO:0000303|PubMed:8464707"
FT /id="VSP_005326"
FT VAR_SEQ 223..383
FT /note="Missing (in isoform 5 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:8464707,
FT ECO:0000303|PubMed:8509359"
FT /id="VSP_007332"
FT VAR_SEQ 223..346
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1469058,
FT ECO:0000303|PubMed:8464707"
FT /id="VSP_007331"
FT VAR_SEQ 223..303
FT /note="Missing (in isoform 3 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:8464707"
FT /id="VSP_007330"
FT VAR_SEQ 223..264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8464707"
FT /id="VSP_007329"
FT VAR_SEQ 424..504
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:8464707"
FT /id="VSP_007334"
FT VAR_SEQ 463..504
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:8509359"
FT /id="VSP_007335"
FT VAR_SEQ 569..592
FT /note="TKSSAKDARRGGSLPTDTTTSVEG -> VRIIKSNWLLSRNQDVMGVSGGGC
FT (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_007338"
FT VAR_SEQ 569..580
FT /note="TKSSAKDARRGG -> VCLVVVADFSAL (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_007336"
FT VAR_SEQ 581..778
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_007337"
FT VAR_SEQ 593..778
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_007339"
FT VAR_SEQ 638
FT /note="G -> R (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:2403559,
FT ECO:0000303|PubMed:2681416, ECO:0000303|PubMed:2682651"
FT /id="VSP_007333"
FT VARIANT 21
FT /note="H -> HPH (in Ly-24.2)"
FT /evidence="ECO:0000269|PubMed:2682651"
FT VARIANT 194
FT /note="G -> S (in Ly-24.2)"
FT /evidence="ECO:0000269|PubMed:2682651"
FT MUTAGEN 715..717
FT /note="KKK->QIN: Loss of interaction with EZR, MSN and RDX
FT and co-localization to microvilli with EZR, MSN and RDX."
FT /evidence="ECO:0000269|PubMed:9472040"
FT CONFLICT 326
FT /note="T -> K (in Ref. 4 and 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="T -> S (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="Y -> H (in Ref. 4, 8 and 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="S -> G (in Ref. 4, 8 and 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="D -> RD (in Ref. 7)"
FT /evidence="ECO:0000305"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:5SBQ"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5SBQ"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:5SBQ"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:5SBQ"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:5SBQ"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5SBQ"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:5SBQ"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:5SBQ"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5SBQ"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:5SBQ"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:5SBQ"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5SBQ"
FT STRAND 715..719
FT /evidence="ECO:0007829|PDB:2ZPY"
SQ SEQUENCE 778 AA; 85617 MW; BD2C073250F6C956 CRC64;
MDKFWWHTAW GLCLLQLSLA HQQIDLNVTC RYAGVFHVEK NGRYSISRTE AADLCQAFNS
TLPTMDQMKL ALSKGFETCR YGFIEGNVVI PRIHPNAICA ANHTGVYILV TSNTSHYDTY
CFNASAPPEE DCTSVTDLPN SFDGPVTITI VNRDGTRYSK KGEYRTHQED IDASNIIDDD
VSSGSTIEKS TPEGYILHTY LPTEQPTGDQ DDSFFIRSTL ATIASTVHSK SHAAAQKQNN
WIWSWFGNSQ STTQTQEPTT SATTALMTTP ETPPKRQEAQ NWFSWLFQPS ESKSHLHTTT
KMPGTESNTN PTGWEPNEEN EDETDTYPSF SGSGIDDDED FISSTIATTP RVSARTEDNQ
DWTQWKPNHS NPEVLLQTTT RMADIDRIST SAHGENWTPE PQPPFNNHEY QDEEETPHAT
STTPNSTAEA AATQQETWFQ NGWQGKNPPT PSEDSHVTEG TTASAHNNHP SQRITTQSQE
DVSWTDFFDP ISHPMGQGHQ TESKDTDSSH STTLQPTAAP NTHLVEDLNR TGPLSVTTPQ
SHSQNFSTLH GEPEEDENYP TTSILPSSTK SSAKDARRGG SLPTDTTTSV EGYTFQYPDT
MENGTLFPVT PAKTEVFGET EVTLATDSNV NVDGSLPGDR DSSKDSRGSS RTVTHGSELA
GHSSANQDSG VTTTSGPMRR PQIPEWLIIL ASLLALALIL AVCIAVNSRR RCGQKKKLVI
NGGNGTVEDR KPSELNGEAS KSQEMVHLVN KEPSETPDQC MTADETRNLQ SVDMKIGV
