Q9Z0M6 (CD97_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CD97 antigen

Alternative name(s):
CD_antigen=CD97

Gene names

Name:

Cd97

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	818 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration. Ref.5
Subunit structure	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 1) do not interact with DAF. Interacts also with chondroitin sulfate By similarity. Ref.2
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.2.
Tissue specificity	Although predominantly expressed by cells of the immune system is expressed ubiquitously, with particularly high levels of expression in the lung and the thymus gland. In the spleen, expression is detected on most myeloid cells and variable portions of T-cells, B-cells and NK cells. In the bone marrow, expressed in nearly all myeloid cells, whereas little if any expression is found on erythroid cells.
Induction	Up-regulated 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 By similarity. Binding to chondroitin sulfate is mediated by the fourth EGF domain By similarity.
Post-translational modification	Proteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane subunit By similarity.
Sequence similarities	Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily. Contains 4 EGF-like domains. Contains 1 GPS domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW neuropeptide signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Traceable author statement PubMed 10501980. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	G-protein coupled receptor activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: InterPro transmembrane signaling receptor activity Traceable author statement PubMed 10501980. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Z0M6-1)

Also known as: EGF(1,2,X,3,4);

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9Z0M6-2)

Also known as: EGF(1,2,4);

The sequence of this isoform differs from the canonical sequence as follows:
     120-213: Missing.

Isoform 3 (identifier: Q9Z0M6-3)

Also known as: EGF(1,2,3,4);

The sequence of this isoform differs from the canonical sequence as follows:
     120-164: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 818	795	CD97 antigen		PRO_0000012869
Regions
	Topological domain	24 – 533	510	Extracellular Potential
	Transmembrane	534 – 554	21	Helical; Name=1; Potential
	Topological domain	555 – 562	8	Cytoplasmic Potential
	Transmembrane	563 – 583	21	Helical; Name=2; Potential
	Topological domain	584 – 602	19	Extracellular Potential
	Transmembrane	603 – 623	21	Helical; Name=3; Potential
	Topological domain	624 – 637	14	Cytoplasmic Potential
	Transmembrane	638 – 658	21	Helical; Name=4; Potential
	Topological domain	659 – 679	21	Extracellular Potential
	Transmembrane	680 – 700	21	Helical; Name=5; Potential
	Topological domain	701 – 723	23	Cytoplasmic Potential
	Transmembrane	724 – 744	21	Helical; Name=6; Potential
	Topological domain	745 – 752	8	Extracellular Potential
	Transmembrane	753 – 773	21	Helical; Name=7; Potential
	Topological domain	774 – 818	45	Cytoplasmic Potential
	Domain	27 – 68	42	EGF-like 1
	Domain	69 – 119	51	EGF-like 2; calcium-binding Potential
	Domain	165 – 213	49	EGF-like 3; calcium-binding Potential
	Domain	214 – 261	48	EGF-like 4; calcium-binding Potential
	Domain	479 – 524	46	GPS
Sites
	Site	513 – 514	2	Cleavage By similarity
Amino acid modifications
	Modified residue	814	1	Phosphoserine By similarity
	Modified residue	816	1	Phosphoserine By similarity
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	227	1	N-linked (GlcNAc...) Potential
	Glycosylation	299	1	N-linked (GlcNAc...) Ref.6 Ref.7
	Glycosylation	395	1	N-linked (GlcNAc...) Ref.6 Ref.7
	Glycosylation	407	1	N-linked (GlcNAc...) Ref.6 Ref.7
	Glycosylation	461	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	502	1	N-linked (GlcNAc...) Potential
	Disulfide bond	31 ↔ 41		By similarity
	Disulfide bond	35 ↔ 47		By similarity
	Disulfide bond	49 ↔ 67		By similarity
	Disulfide bond	73 ↔ 86		By similarity
	Disulfide bond	80 ↔ 95		By similarity
	Disulfide bond	97 ↔ 118		By similarity
	Disulfide bond	169 ↔ 182		By similarity
	Disulfide bond	176 ↔ 191		By similarity
	Disulfide bond	193 ↔ 212		By similarity
	Disulfide bond	218 ↔ 231		By similarity
	Disulfide bond	225 ↔ 240		By similarity
	Disulfide bond	242 ↔ 260		By similarity
Natural variations
	Alternative sequence	120 – 213	94	Missing in isoform 2.		VSP_009413
	Alternative sequence	120 – 164	45	Missing in isoform 3.		VSP_009414
Experimental info
	Sequence conflict	3	1	G → S in CAB38246. Ref.1
	Sequence conflict	28	1	S → I in CAB38246. Ref.1
	Sequence conflict	320	1	Q → E in AAH06676. Ref.3
	Sequence conflict	506	1	F → S in AAF67800. Ref.2
	Sequence conflict	599	1	M → V in AAH06676. Ref.3
	Sequence conflict	726	1	A → S Ref.3
	Sequence conflict	726	1	A → S Ref.4
	Sequence conflict	796	1	F → I in BAB25461. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (EGF(1,2,X,3,4)) [UniParc]. Last modified February 16, 2004. Version 2. Checksum: E59A292F2CF626C2	FASTA	818	90,413
	10 20 30 40 50 60 MRGVRCPGLL VVCILLSLSG AGTQKAESKN CAKWCPINSK CVSNRSCVCK PGFSSEKELI 70 80 90 100 110 120 TNPAESCEDI NECLLPGFSC GDFAMCKNSE GSYTCVCNLG YKLLSGAESF VNESENTCQA 130 140 150 160 170 180 SVNTGTTPVP SRIHTVTTAP GNLPEQTTTV HQTQMGDSEE RTPKDVNECI SGQNHCHQST 190 200 210 220 230 240 HCINKLGGYS CICRQGWKPV PGSPNGPVST VCEDVDECSS GQHQCHNSTV CKNTVGSYKC 250 260 270 280 290 300 HCRPGWKPTS GSLRGPDTIC QEPPFPTWTL LPTAHSQTLL RFSVEVQNLL RDFNPATVNY 310 320 330 340 350 360 TIQKLIEAVD KLLEDPMETQ TQQVAAQLLS NLEQSLRTLA QFLPKGPFTY TSPSNTELSL 370 380 390 400 410 420 MVKEQDNKDV TTVHHGQTWM ELDWAVTAGA KISENGSSVA GILSSPNMEK LLGNTPLNLE 430 440 450 460 470 480 QRRASLEDFY GSPIPSVSLK LLSNINSVFL TNTNTEKLAS NVTFKFDFTS VESIEPRHEL 490 500 510 520 530 540 ICAFWKAHNG NGYWDTDGCS MNGTGFCHCN HLTSFAILMA QYHVQDPRLE LITKVGLLLS 550 560 570 580 590 600 LICLLLCILT FLLVKPIQSS RTMVHLHLCI CLFLGSIIFL VGVENEGGEV GLRCRLVAMM 610 620 630 640 650 660 LHFCFLAAFC WMALEGVELY FLVVRVFQGQ GLSTWQRCLI GYGVPLLIVA ISMAVVKMDG 670 680 690 700 710 720 YGHATYCWLD FRKQGFLWSF SGPVAFIIFC NAAIFVITVW KLTKKFSEIN PNMKKLRKAR 730 740 750 760 770 780 VLTITAIAQL LVLGCTWGFG LFLFNPHSTW LSYIFTLLNC LQGLFLYVML CLLNKKVREE 790 800 810 YWKWACMVTG SKYTEFNSST TGTGTSQTRA LRSSESGM
	Isoform 2 (EGF(1,2,4)) [UniParc]. Checksum: 7DA1962863ED5A5F	FASTA	724	80,433
	10 20 30 40 50 60 MRGVRCPGLL VVCILLSLSG AGTQKAESKN CAKWCPINSK CVSNRSCVCK PGFSSEKELI 70 80 90 100 110 120 TNPAESCEDI NECLLPGFSC GDFAMCKNSE GSYTCVCNLG YKLLSGAESF VNESENTCQD 130 140 150 160 170 180 VDECSSGQHQ CHNSTVCKNT VGSYKCHCRP GWKPTSGSLR GPDTICQEPP FPTWTLLPTA 190 200 210 220 230 240 HSQTLLRFSV EVQNLLRDFN PATVNYTIQK LIEAVDKLLE DPMETQTQQV AAQLLSNLEQ 250 260 270 280 290 300 SLRTLAQFLP KGPFTYTSPS NTELSLMVKE QDNKDVTTVH HGQTWMELDW AVTAGAKISE 310 320 330 340 350 360 NGSSVAGILS SPNMEKLLGN TPLNLEQRRA SLEDFYGSPI PSVSLKLLSN INSVFLTNTN 370 380 390 400 410 420 TEKLASNVTF KFDFTSVESI EPRHELICAF WKAHNGNGYW DTDGCSMNGT GFCHCNHLTS 430 440 450 460 470 480 FAILMAQYHV QDPRLELITK VGLLLSLICL LLCILTFLLV KPIQSSRTMV HLHLCICLFL 490 500 510 520 530 540 GSIIFLVGVE NEGGEVGLRC RLVAMMLHFC FLAAFCWMAL EGVELYFLVV RVFQGQGLST 550 560 570 580 590 600 WQRCLIGYGV PLLIVAISMA VVKMDGYGHA TYCWLDFRKQ GFLWSFSGPV AFIIFCNAAI 610 620 630 640 650 660 FVITVWKLTK KFSEINPNMK KLRKARVLTI TAIAQLLVLG CTWGFGLFLF NPHSTWLSYI 670 680 690 700 710 720 FTLLNCLQGL FLYVMLCLLN KKVREEYWKW ACMVTGSKYT EFNSSTTGTG TSQTRALRSS ESGM
	Isoform 3 (EGF(1,2,3,4)) [UniParc]. Checksum: E18D892177ECC3F9	FASTA	773	85,657
	10 20 30 40 50 60 MRGVRCPGLL VVCILLSLSG AGTQKAESKN CAKWCPINSK CVSNRSCVCK PGFSSEKELI 70 80 90 100 110 120 TNPAESCEDI NECLLPGFSC GDFAMCKNSE GSYTCVCNLG YKLLSGAESF VNESENTCQD 130 140 150 160 170 180 VNECISGQNH CHQSTHCINK LGGYSCICRQ GWKPVPGSPN GPVSTVCEDV DECSSGQHQC 190 200 210 220 230 240 HNSTVCKNTV GSYKCHCRPG WKPTSGSLRG PDTICQEPPF PTWTLLPTAH SQTLLRFSVE 250 260 270 280 290 300 VQNLLRDFNP ATVNYTIQKL IEAVDKLLED PMETQTQQVA AQLLSNLEQS LRTLAQFLPK 310 320 330 340 350 360 GPFTYTSPSN TELSLMVKEQ DNKDVTTVHH GQTWMELDWA VTAGAKISEN GSSVAGILSS 370 380 390 400 410 420 PNMEKLLGNT PLNLEQRRAS LEDFYGSPIP SVSLKLLSNI NSVFLTNTNT EKLASNVTFK 430 440 450 460 470 480 FDFTSVESIE PRHELICAFW KAHNGNGYWD TDGCSMNGTG FCHCNHLTSF AILMAQYHVQ 490 500 510 520 530 540 DPRLELITKV GLLLSLICLL LCILTFLLVK PIQSSRTMVH LHLCICLFLG SIIFLVGVEN 550 560 570 580 590 600 EGGEVGLRCR LVAMMLHFCF LAAFCWMALE GVELYFLVVR VFQGQGLSTW QRCLIGYGVP 610 620 630 640 650 660 LLIVAISMAV VKMDGYGHAT YCWLDFRKQG FLWSFSGPVA FIIFCNAAIF VITVWKLTKK 670 680 690 700 710 720 FSEINPNMKK LRKARVLTIT AIAQLLVLGC TWGFGLFLFN PHSTWLSYIF TLLNCLQGLF 730 740 750 760 770 LYVMLCLLNK KVREEYWKWA CMVTGSKYTE FNSSTTGTGT SQTRALRSSE SGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of mouse CD97." Hamann J., van Zventer C., Bijl A., Molenaar C., Tesselaar K., van Lier R.A.W. Int. Immunol. 12:439-448(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[2]	"Structural characterization of mouse CD97 and study of its specific interaction with the murine decay-accelerating factor (DAF, CD55)." Qian Y.-M., Haino M., Kelly K., Song W.-C. Immunology 98:303-311(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH DAF, SUBCELLULAR LOCATION. Tissue: Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 607-818. Strain: C57BL/6J. Tissue: Small intestine.
[5]	"The epidermal growth factor-seven transmembrane (EGF-TM7) receptor CD97 is required for neutrophil migration and host defense." Leemans J.C., te Velde A.A., Florquin S., Bennink R.J., de Bruin K., van Lier R.A.W., van der Poll T., Hamann J. J. Immunol. 172:1125-1131(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299; ASN-395; ASN-407 AND ASN-461, MASS SPECTROMETRY. Tissue: Myoblast.
[7]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299; ASN-395 AND ASN-407, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y18365 mRNA. Translation: CAB38246.1. AF146344 mRNA. Translation: AAF67800.1. BC006676 mRNA. Translation: AAH06676.1. AK008101 mRNA. Translation: BAB25461.1.
IPI	IPI00399798. IPI00399799. IPI00399800.
RefSeq	NP_001156501.1. NM_001163029.1.
UniGene	Mm.334648.
3D structure databases
ProteinModelPortal	Q9Z0M6.
SMR	Q9Z0M6. Positions 31-261.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000075240.
Protein family/group databases
MEROPS	S63.036.
GPCRDB	Search...
PTM databases
PhosphoSite	Q9Z0M6.
Proteomic databases
PaxDb	Q9Z0M6.
PRIDE	Q9Z0M6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000002964; ENSMUSP00000002964; ENSMUSG00000002885.
GeneID	26364.
KEGG	mmu:26364.
UCSC	uc009mlc.2. mouse. uc012ggt.1. mouse.
Organism-specific databases
CTD	976.
MGI	MGI:1347095. Cd97.
Phylogenomic databases
eggNOG	NOG320737.
GeneTree	ENSGT00650000093107.
HOGENOM	HOG000294115.
HOVERGEN	HBG048917.
InParanoid	Q9Z0M6.
KO	K08446.
OrthoDB	EOG45X7WF.
Gene expression databases
ArrayExpress	Q9Z0M6.
Bgee	Q9Z0M6.
CleanEx	MM_CD97.
Genevestigator	Q9Z0M6.
GermOnline	ENSMUSG00000002885. Mus musculus.
Family and domain databases
InterPro	IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR017981. GPCR_2-like. IPR003056. GPCR_2_CD97. IPR000832. GPCR_2_secretin-like. IPR000203. GPS_dom. [Graphical view]
Pfam	PF00002. 7tm_2. 1 hit. PF07645. EGF_CA. 3 hits. PF01825. GPS. 1 hit. [Graphical view]
PRINTS	PR01278. CD97PROTEIN. PR00249. GPCRSECRETIN.
SMART	SM00181. EGF. 1 hit. SM00179. EGF_CA. 3 hits. SM00303. GPS. 1 hit. [Graphical view]
PROSITE	PS00010. ASX_HYDROXYL. 3 hits. PS50026. EGF_3. 3 hits. PS01187. EGF_CA. 3 hits. PS00650. G_PROTEIN_RECEP_F2_2. False negative. PS50261. G_PROTEIN_RECEP_F2_4. 1 hit. PS50221. GPS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CD97. mouse.
NextBio	304231.
SOURCE	Search...

Entry information

Entry name

CD97_MOUSE

Accession

Primary (citable) accession number: Q9Z0M6
Secondary accession number(s): Q923A1, Q9CVI5, Q9JLQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
Last sequence update:	February 16, 2004
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program