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UniProtKB/Swiss-Prot entry P48960


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CD97_HUMAN
Primary accession number P48960
Secondary accession numbers O00718 O76101 Q8NG72 Q8TBQ7
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on March 21, 2006 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 101)
Name and origin of the protein
Protein name CD97 antigen [Precursor]
Synonyms Leukocyte antigen CD97
CD97 antigen
Contains CD97 antigen subunit alpha
CD97 antigen subunit beta
Gene name
Name: CD97
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=7636245 [NCBI, ExPASy, EBI, Israel, Japan]
Hamann J., Eichler W., Hamann D., Kerstens H.M.J., Poddighe P.J., Hoovers J.M.N., Hartmann J.M., Strauss M., van Lier R.A.W.;
"Expression cloning and chromosomal mapping of the leukocyte activation antigen CD97, a new seven-span transmembrane molecule of the secretion receptor superfamily with an unusual extracellular domain.";
J. Immunol. 155:1942-1950(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Foreskin;
DOI=10.1006/geno.1996.0092; PubMed=8786105 [NCBI, ExPASy, EBI, Israel, Japan]
Hamann J., Hartmann E., van Lier R.A.W.;
"Structure of the human CD97 gene: exon shuffling has generated a new type of seven-span transmembrane molecule related to the secretin receptor superfamily.";
Genomics 32:144-147(1996).
[3]
SEQUENCE REVISION.
Hamann J.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=8955192 [NCBI, ExPASy, EBI, Israel, Japan]
Gray J.X., Haino M., Roth M.J., Maguire J.E., Jensen P.N., Yarme A., Stetler-Stevenson M.-A., Siebenlist U., Kelly K.;
"CD97 is a processed, seven-transmembrane, heterodimeric receptor associated with inflammation.";
J. Immunol. 157:5438-5447(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon adenocarcinoma;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH DAF.
DOI=10.1074/jbc.M101770200; PubMed=11297558 [NCBI, ExPASy, EBI, Israel, Japan]
Lin H.-H., Stacey M., Saxby C., Knott V., Chaudhry Y., Evans D., Gordon S., McKnight A.J., Handford P., Lea S.;
"Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: dissection of the CD97-CD55 complex.";
J. Biol. Chem. 276:24160-24169(2001).
[9]
INTERACTION WITH CHONDROITIN SULFATE.
DOI=10.1182/blood-2002-11-3540; PubMed=12829604 [NCBI, ExPASy, EBI, Israel, Japan]
Stacey M., Chang G.-W., Davies J.Q., Kwakkenbos M.J., Sanderson R.D., Hamann J., Gordon S., Lin H.-H.;
"The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans.";
Blood 102:2916-2924(2003).
[10]
REVIEW.
DOI=10.1007/s00251-003-0625-2; PubMed=14647991 [NCBI, ExPASy, EBI, Israel, Japan]
Kwakkenbos M.J., Kop E.N., Stacey M., Matmati M., Gordon S., Lin H.H., Hamann J.;
"The EGF-TM7 family: a postgenomic view.";
Immunogenetics 55:655-666(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-818 AND SER-831, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831 AND SER-833, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-453, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
Comments
  • FUNCTION: Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration (By similarity).
  • SUBUNIT: Forms a heterodimer, consisting of a large extracellular region (alpha subunit) non-covalently linked to a seven-transmembrane moiety (beta subunit). Interacts with complement decay-accelerating factor (DAF). The largest isoform (isoform 1) interacts with chondroitin sulfate.
  • INTERACTION:
    P12931:SRC; NbExp=1; IntAct=EBI-1756009, EBI-621482;
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
  • SUBCELLULAR LOCATION: CD97 antigen subunit alpha: Secreted, extracellular space.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsEGF(1,2,3,4,5)
    Isoform IDP48960-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsEGF(1,2,5)
    Isoform IDP48960-2
    Features which should be applied to build the isoform sequence: VSP_009411.
    Name3
    SynonymsEGF(1,2,3,5)
    Isoform IDP48960-3
    Features which should be applied to build the isoform sequence: VSP_009412.
  • TISSUE SPECIFICITY: Broadly expressed, found on most hematopoietic cells, including activated lymphocytes, monocytes, macrophages, dendritic cells, and granulocytes. Expressed also abundantly by smooth muscle cells. Expressed in thyroid, colorectal, gastric, esophageal and pancreatic carcinomas too. Expression are increased under inflammatory conditions in the CNS of multiple sclerosis and in synovial tissue of patients with rheumatoid arthritis. Increased expression of CD97 in the synovium is accompagnied by detectable levels of soluble CD97 in the synovial fluid.
  • INDUCTION: Rapid up-regulation during lymphocyte activation.
  • DOMAIN: The first two EGF domains mediate the interaction with DAF. A third tandemly arranged EGF domain is necessary for the structural integrity of the binding region.
  • DOMAIN: Binding to chondroitin sulfate is mediated by the fourth EGF domain.
  • PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane subunit (By similarity).
  • SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily [view classification].
  • SIMILARITY: Contains 5 EGF-like domains.
  • SIMILARITY: Contains 1 GPS domain.
  • SEQUENCE CAUTION:
    • Sequence=AAC27673.1; Type=Erroneous gene model prediction;
    • Sequence=BAC06178.1; Type=Erroneous gene model prediction;
  • WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CD97ID996ch19p13.html";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X84700; CAA59173.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94630; CAA64333.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94631; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94632; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94633; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99830; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99831; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94634; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94635; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94636; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94637; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94638; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94639; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94640; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94641; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94642; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94643; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94644; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94645; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94646; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94647; CAA64333.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U76764; AAB36682.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB065966; BAC06178.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005327; AAC27673.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026690; AAH26690.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00299412; -.
IPI00397229; -.
IPI00397230; -.
PIR I37225; I37225.
RefSeq NP_001020331.1; -.
NP_001775.2; -.
NP_510966.1; -.
UniGene Hs.466039
3D structure databases
HSSP P16109; 1FSB. [HSSP ENTRY / PDB]
ModBase P48960.
Protein-protein interaction databases
IntAct P48960; 1.
Protein family/group databases
GPCRDB P48960; CD97_HUMAN.
PTM databases
PhosphoSite P48960; -.
Organism-specific databases
GeneCards GC19P014353; -.
H-InvDB HIX0014835; -.
HGNC HGNC:1711; CD97.
GenAtlas CD97.
HPA HPA013707; -.
MIM 601211; gene. [NCBI / EBI]
PharmGKB PA26248; -.
Gene expression databases
Bgee P48960; -.
CleanEx HS_CD97; -.
GermOnline ENSG00000123146; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004930; Molecular function: G-protein coupled receptor activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007155; Biological process: cell adhesion (traceable author statement from ProtInc).
GO:0006928; Biological process: cell motion (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (traceable author statement from ProtInc).
GO:0006954; Biological process: inflammatory response (traceable author statement from ProtInc).
GO:0007218; Biological process: neuropeptide signaling pathway (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR013091; EGF_Ca_bd_2.
IPR018097; EGF_Ca_bd_CS.
IPR017981; GPCR_2-like.
IPR003056; GPCR_2_CD97.
IPR000832; GPCR_2_secretin-like.
IPR017983; GPCR_2_secretin-like_CS.
IPR000203; PKD_cys_rich.
Graphical view of domain structure.
Pfam PF00002; 7tm_2; 1.
PF07645; EGF_CA; 4.
PF01825; GPS; 1.
Pfam graphical view of domain structure.
PRINTS PR01278; CD97PROTEIN.
PR00249; GPCRSECRETIN.
SMART SM00179; EGF_CA; 4.
SM00303; GPS; 1.
SMART graphical view of domain structure.
PROSITE PS00010; ASX_HYDROXYL; 4.
PS50026; EGF_3; 4.
PS01187; EGF_CA; 4.
PS00650; G_PROTEIN_RECEP_F2_2; 1.
PS50261; G_PROTEIN_RECEP_F2_4; 1.
PS50221; GPS; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P48960; -.
Genome annotation databases
Ensembl ENSG00000123146; Homo sapiens. [Contig view]
GeneID 976; -.
KEGG hsa:976; -.
NMPDR fig|9606.3.peg.15845; -.
Phylogenomic databases
HOGENOM P48960; -.
HOVERGEN P48960; -.
OMA P48960; QVGLRCR.
Other
NextBio 4094; -.
SOURCE CD97; Homo sapiens.
GPCRDB-Snakes P48960.
ProtoNet P48960.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Calcium; Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain; G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Receptor; Repeat; Secreted; Signal; Transducer; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     Potential. 
CHAIN   21   835  815     CD97 antigen. PRO_0000012868
CHAIN   21   530  510     CD97 antigen subunit alpha (By similarity). PRO_0000296235
CHAIN   531   835  305     CD97 antigen subunit beta (By similarity). PRO_0000296236
TOPO_DOM   21   552  532     Extracellular (Potential). 
TRANSMEM   553   572  20     1 (Potential). 
TOPO_DOM   573   581  9     Cytoplasmic (Potential). 
TRANSMEM   582   601  20     2 (Potential). 
TOPO_DOM   602   620  19     Extracellular (Potential). 
TRANSMEM   621   642  22     3 (Potential). 
TOPO_DOM   643   653  11     Cytoplasmic (Potential). 
TRANSMEM   654   674  21     4 (Potential). 
TOPO_DOM   675   691  17     Extracellular (Potential). 
TRANSMEM   692   712  21     5 (Potential). 
TOPO_DOM   713   739  27     Cytoplasmic (Potential). 
TRANSMEM   740   760  21     6 (Potential). 
TOPO_DOM   761   766  6     Extracellular (Potential). 
TRANSMEM   767   789  23     7 (Potential). 
TOPO_DOM   790   835  46     Cytoplasmic (Potential). 
DOMAIN   22    63  42     EGF-like 1. 
DOMAIN   64   115  52     EGF-like 2; calcium-binding (Potential). 
DOMAIN   116   159  44     EGF-like 3; calcium-binding (Potential). 
DOMAIN   160   208  49     EGF-like 4; calcium-binding (Potential). 
DOMAIN   209   257  49     EGF-like 5; calcium-binding (Potential). 
DOMAIN   492   542  51     GPS. 
SITE   530   531  2     Cleavage (By similarity). 
MOD_RES   818   818        Phosphoserine. 
MOD_RES   831   831        Phosphoserine. 
MOD_RES   833   833        Phosphoserine. 
CARBOHYD   33    33        N-linked (GlcNAc...) (Potential). 
CARBOHYD   38    38        N-linked (GlcNAc...) (Potential). 
CARBOHYD   108   108        N-linked (GlcNAc...) (Potential). 
CARBOHYD   203   203        N-linked (GlcNAc...) (Potential). 
CARBOHYD   371   371        N-linked (GlcNAc...) (Potential). 
CARBOHYD   406   406        N-linked (GlcNAc...) (Potential). 
CARBOHYD   413   413        N-linked (GlcNAc...) (Potential). 
CARBOHYD   453   453        N-linked (GlcNAc...). 
CARBOHYD   520   520        N-linked (GlcNAc...) (Potential). 
DISULFID   26    36        By similarity. 
DISULFID   30    42        By similarity. 
DISULFID   44    62        By similarity. 
DISULFID   68    82        By similarity. 
DISULFID   76    91        By similarity. 
DISULFID   93   114        By similarity. 
DISULFID   120   133        By similarity. 
DISULFID   127   142        By similarity. 
DISULFID   144   158        By similarity. 
DISULFID   164   177        By similarity. 
DISULFID   171   186        By similarity. 
DISULFID   188   207        By similarity. 
DISULFID   213   226        By similarity. 
DISULFID   220   235        By similarity. 
DISULFID   237   256        By similarity. 
VAR_SEQ   116   208        Missing (in isoform 2). VSP_009411
VAR_SEQ   160   208        Missing (in isoform 3). VSP_009412
VARIANT   367   367  1     R -> Q (in dbSNP:rs2230748 [NCBI]). VAR_017760 
CONFLICT   103   103        A -> T (in Ref. 4; AAB36682). 
CONFLICT   512   512        G -> V (in Ref. 1 and 2). 
CONFLICT   534   534        A -> T (in Ref. 1 and 2). 
Sequence information
Length: 835 AA [This is the length of the unprocessed precursor] Molecular weight: 91869 Da [This is the MW of the unprocessed precursor] CRC64: 06DDDE9178BC494B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGGRVFLAFC VWLTLPGAET QDSRGCARWC PQNSSCVNAT ACRCNPGFSS FSEIITTPTE 

        70         80         90        100        110        120 
TCDDINECAT PSKVSCGKFS DCWNTEGSYD CVCSPGYEPV SGAKTFKNES ENTCQDVDEC 

       130        140        150        160        170        180 
QQNPRLCKSY GTCVNTLGSY TCQCLPGFKF IPEDPKVCTD VNECTSGQNP CHSSTHCLNN 

       190        200        210        220        230        240 
VGSYQCRCRP GWQPIPGSPN GPNNTVCEDV DECSSGQHQC DSSTVCFNTV GSYSCRCRPG 

       250        260        270        280        290        300 
WKPRHGIPNN QKDTVCEDMT FSTWTPPPGV HSQTLSRFFD KVQDLGRDSK TSSAEVTIQN 

       310        320        330        340        350        360 
VIKLVDELME APGDVEALAP PVRHLIATQL LSNLEDIMRI LAKSLPKGPF TYISPSNTEL 

       370        380        390        400        410        420 
TLMIQERGDK NVTMGQSSAR MKLNWAVAAG AEDPGPAVAG ILSIQNMTTL LANASLNLHS 

       430        440        450        460        470        480 
KKQAELEEIY ESSIRGVQLR RLSAVNSIFL SHNNTKELNS PILFAFSHLE SSDGEAGRDP 

       490        500        510        520        530        540 
PAKDVMPGPR QELLCAFWKS DSDRGGHWAT EGCQVLGSKN GSTTCQCSHL SSFAILMAHY 

       550        560        570        580        590        600 
DVEDWKLTLI TRVGLALSLF CLLLCILTFL LVRPIQGSRT TIHLHLCICL FVGSTIFLAG 

       610        620        630        640        650        660 
IENEGGQVGL RCRLVAGLLH YCFLAAFCWM SLEGLELYFL VVRVFQGQGL STRWLCLIGY 

       670        680        690        700        710        720 
GVPLLIVGVS AAIYSKGYGR PRYCWLDFEQ GFLWSFLGPV TFIILCNAVI FVTTVWKLTQ 

       730        740        750        760        770        780 
KFSEINPDMK KLKKARALTI TAIAQLFLLG CTWVFGLFIF DDRSLVLTYV FTILNCLQGA 

       790        800        810        820        830 
FLYLLHCLLN KKVREEYRKW ACLVAGGSKY SEFTSTTSGT GHNQTRALRA SESGI 

P48960 in FASTA format

View entry in raw text format (no links)
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