Q8CA95 (PDE10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
EC=3.1.4.17
EC=3.1.4.35

Gene names

Name:

Pde10a

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	790 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition. Ref.1
Catalytic activity	Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate. Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.
Cofactor	Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions By similarity.
Pathway	Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Detected in striatum (at protein level). Detected in testis and brain. Ref.1 Ref.2
Induction	Down-regulated by the expression of a huntingtin (HD) gene with an expanded polyglutamine repeat prior to the onset of neurological symptoms related to Huntington disease. Ref.2
Domain	The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity By similarity. Composed of a C-terminal catalytic domain containing two divalent metal sites and an N-terminal regulatory domain which contains one cyclic nucleotide-binding region By similarity.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family.
Biophysicochemical properties	Kinetic parameters: KM=0.05 µM for cAMP Ref.1 KM=3 µM for cGMP

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Metal-binding Nucleotide-binding cAMP cAMP-binding cGMP cGMP-binding
Molecular function	Hydrolase
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cAMP catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cGMP catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of cAMP-mediated signaling Inferred from mutant phenotype PubMed 18923023. Source: MGI regulation of protein kinase A signaling cascade Inferred from mutant phenotype PubMed 18923023. Source: MGI signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC cAMP binding Inferred from sequence or structural similarity. Source: UniProtKB cGMP binding Inferred from electronic annotation. Source: UniProtKB-KW cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8CA95-1)

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: Q8CA95-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MSNDSTEGTVGSCNAT → MEKLY

Isoform 3 (identifier: Q8CA95-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MSNDSTEGTVGSCNATG → MEDGPSNNASCFRRLTECFLSPS

Isoform 4 (identifier: Q8CA95-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.
     61-69: EPSPKEVSR → MPGPGQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 790	790	cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A		PRO_0000355558
Regions
	Region	290 – 291	2	Allosteric effector binding By similarity
	Region	334 – 335	2	Allosteric effector binding By similarity
Sites
	Active site	519	1	Proton donor By similarity
	Metal binding	523	1	Divalent metal cation 1 By similarity
	Metal binding	557	1	Divalent metal cation 1 By similarity
	Metal binding	558	1	Divalent metal cation 1 By similarity
	Metal binding	558	1	Divalent metal cation 2 By similarity
	Metal binding	668	1	Divalent metal cation 1 By similarity
	Binding site	368	1	Allosteric effector By similarity
	Binding site	387	1	Allosteric effector By similarity
	Binding site	519	1	Substrate By similarity
	Binding site	720	1	Substrate By similarity
Natural variations
	Alternative sequence	1 – 60	60	Missing in isoform 4.		VSP_035915
	Alternative sequence	1 – 17	17	MSNDS…CNATG → MEDGPSNNASCFRRLTECFL SPS in isoform 3.		VSP_035916
	Alternative sequence	1 – 16	16	MSNDS…SCNAT → MEKLY in isoform 2.		VSP_035917
	Alternative sequence	61 – 69	9	EPSPKEVSR → MPGPGQ in isoform 4.		VSP_035918
Experimental info
	Sequence conflict	774	1	P → Q in BAC30292. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 1B1D8111A5AD7B92	FASTA	790	89,408
	10 20 30 40 50 60 MSNDSTEGTV GSCNATGLTD EKVKAYLSLH PQVLDEFVSE SVSAETVEKW LKRKTNKAKD 70 80 90 100 110 120 EPSPKEVSRY QDTNMQGVVY ELNSYIEQRL DTGGDNHLLL YELSSIIRIA TKADGFALYF 130 140 150 160 170 180 LGECNNSLCV FIPPGMKEGQ PRLIPAGPIT QGTTISAYVA KSRKTLLVED ILGDERFPRG 190 200 210 220 230 240 TGLESGTRIQ SVLCLPIVTA IGDLIGILEL YRHWGKEAFC LSHQEVATAN LAWASVAIHQ 250 260 270 280 290 300 VQVCRGLAKQ TELNDFLLDV SKTYFDNIVA IDSLLEHIMI YAKNLVNADR CALFQVDHKN 310 320 330 340 350 360 KELYSDLFDI GEEKEGKPIF KKTKEIRFSI EKGIAGQVAR TGEVLNIPDA YADPRFNREV 370 380 390 400 410 420 DLYTGYTTRN ILCMPIVSRG SVIGVVQMVN KISGSAFSKT DENNFKMFAV FCALALHCAN 430 440 450 460 470 480 MYHRIRHSEC IYRVTMEKLS YHSICTSEEW QGLMRFNLPA RICRDIELFH FDIGPFENMW 490 500 510 520 530 540 PGIFVYMIHR SCGTSCFELE KLCRFIMSVK KNYRRVPYHN WKHAVTVAHC MYAILQNNNG 550 560 570 580 590 600 LFTDLERKGL LIACLCHDLD HRGFSNSYLQ KFDHPLAALY STSTMEQHHF SQTVSILQLE 610 620 630 640 650 660 GHNIFSTLSS SEYEQVLEII RKAIIATDLA LYFGNRKQLE EMYQTGSLNL HNQSHRDRVI 670 680 690 700 710 720 GLMMTACDLC SVTKLWPVTK LTANDIYAEF WAEGDEMKKL GIQPIPMMDR DKRDEVPQGQ 730 740 750 760 770 780 LGFYNAVAIP CYTTLTQILP PTEPLLKACR DNLNQWEKVI RGEETAMWIS GPGPAPSKST 790 PEKLNVKVED
	Isoform 2 [UniParc]. Checksum: 83691B72F0D0EEAB	FASTA	779	88,517
	10 20 30 40 50 60 MEKLYGLTDE KVKAYLSLHP QVLDEFVSES VSAETVEKWL KRKTNKAKDE PSPKEVSRYQ 70 80 90 100 110 120 DTNMQGVVYE LNSYIEQRLD TGGDNHLLLY ELSSIIRIAT KADGFALYFL GECNNSLCVF 130 140 150 160 170 180 IPPGMKEGQP RLIPAGPITQ GTTISAYVAK SRKTLLVEDI LGDERFPRGT GLESGTRIQS 190 200 210 220 230 240 VLCLPIVTAI GDLIGILELY RHWGKEAFCL SHQEVATANL AWASVAIHQV QVCRGLAKQT 250 260 270 280 290 300 ELNDFLLDVS KTYFDNIVAI DSLLEHIMIY AKNLVNADRC ALFQVDHKNK ELYSDLFDIG 310 320 330 340 350 360 EEKEGKPIFK KTKEIRFSIE KGIAGQVART GEVLNIPDAY ADPRFNREVD LYTGYTTRNI 370 380 390 400 410 420 LCMPIVSRGS VIGVVQMVNK ISGSAFSKTD ENNFKMFAVF CALALHCANM YHRIRHSECI 430 440 450 460 470 480 YRVTMEKLSY HSICTSEEWQ GLMRFNLPAR ICRDIELFHF DIGPFENMWP GIFVYMIHRS 490 500 510 520 530 540 CGTSCFELEK LCRFIMSVKK NYRRVPYHNW KHAVTVAHCM YAILQNNNGL FTDLERKGLL 550 560 570 580 590 600 IACLCHDLDH RGFSNSYLQK FDHPLAALYS TSTMEQHHFS QTVSILQLEG HNIFSTLSSS 610 620 630 640 650 660 EYEQVLEIIR KAIIATDLAL YFGNRKQLEE MYQTGSLNLH NQSHRDRVIG LMMTACDLCS 670 680 690 700 710 720 VTKLWPVTKL TANDIYAEFW AEGDEMKKLG IQPIPMMDRD KRDEVPQGQL GFYNAVAIPC 730 740 750 760 770 YTTLTQILPP TEPLLKACRD NLNQWEKVIR GEETAMWISG PGPAPSKSTP EKLNVKVED
	Isoform 3 [UniParc]. Checksum: 4662D791B45E9EBA	FASTA	796	90,339
	10 20 30 40 50 60 MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK 70 80 90 100 110 120 TNKAKDEPSP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNHLLLYELS SIIRIATKAD 130 140 150 160 170 180 GFALYFLGEC NNSLCVFIPP GMKEGQPRLI PAGPITQGTT ISAYVAKSRK TLLVEDILGD 190 200 210 220 230 240 ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA 250 260 270 280 290 300 SVAIHQVQVC RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF 310 320 330 340 350 360 QVDHKNKELY SDLFDIGEEK EGKPIFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP 370 380 390 400 410 420 RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL 430 440 450 460 470 480 ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM RFNLPARICR DIELFHFDIG 490 500 510 520 530 540 PFENMWPGIF VYMIHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI 550 560 570 580 590 600 LQNNNGLFTD LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV 610 620 630 640 650 660 SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLHNQS 670 680 690 700 710 720 HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKRD 730 740 750 760 770 780 EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLN QWEKVIRGEE TAMWISGPGP 790 APSKSTPEKL NVKVED
	Isoform 4 [UniParc]. Checksum: 703F98A68850E67E	FASTA	727	82,409
	10 20 30 40 50 60 MPGPGQYQDT NMQGVVYELN SYIEQRLDTG GDNHLLLYEL SSIIRIATKA DGFALYFLGE 70 80 90 100 110 120 CNNSLCVFIP PGMKEGQPRL IPAGPITQGT TISAYVAKSR KTLLVEDILG DERFPRGTGL 130 140 150 160 170 180 ESGTRIQSVL CLPIVTAIGD LIGILELYRH WGKEAFCLSH QEVATANLAW ASVAIHQVQV 190 200 210 220 230 240 CRGLAKQTEL NDFLLDVSKT YFDNIVAIDS LLEHIMIYAK NLVNADRCAL FQVDHKNKEL 250 260 270 280 290 300 YSDLFDIGEE KEGKPIFKKT KEIRFSIEKG IAGQVARTGE VLNIPDAYAD PRFNREVDLY 310 320 330 340 350 360 TGYTTRNILC MPIVSRGSVI GVVQMVNKIS GSAFSKTDEN NFKMFAVFCA LALHCANMYH 370 380 390 400 410 420 RIRHSECIYR VTMEKLSYHS ICTSEEWQGL MRFNLPARIC RDIELFHFDI GPFENMWPGI 430 440 450 460 470 480 FVYMIHRSCG TSCFELEKLC RFIMSVKKNY RRVPYHNWKH AVTVAHCMYA ILQNNNGLFT 490 500 510 520 530 540 DLERKGLLIA CLCHDLDHRG FSNSYLQKFD HPLAALYSTS TMEQHHFSQT VSILQLEGHN 550 560 570 580 590 600 IFSTLSSSEY EQVLEIIRKA IIATDLALYF GNRKQLEEMY QTGSLNLHNQ SHRDRVIGLM 610 620 630 640 650 660 MTACDLCSVT KLWPVTKLTA NDIYAEFWAE GDEMKKLGIQ PIPMMDRDKR DEVPQGQLGF 670 680 690 700 710 720 YNAVAIPCYT TLTQILPPTE PLLKACRDNL NQWEKVIRGE ETAMWISGPG PAPSKSTPEK LNVKVED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a dual-substrate phosphodiesterase gene family: PDE10A." Soderling S.H., Bayuga S.J., Beavo J.A. Proc. Natl. Acad. Sci. U.S.A. 96:7071-7076(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY. Tissue: Testis.
[2]	"Striatal phosphodiesterase mRNA and protein levels are reduced in Huntington's disease transgenic mice prior to the onset of motor symptoms." Hebb A.L., Robertson H.A., Denovan-Wright E.M. Neuroscience 123:967-981(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INDUCTION, TISSUE SPECIFICITY. Strain: C57BL/6 X CBA. Tissue: Corpus striatum.
[3]	"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] (ISOFORMS 1 AND 4). Strain: C57BL/6J. Tissue: Mammary gland, Spinal cord and Thymus.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 1).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF110507 mRNA. Translation: AAD31544.1. AY360383 mRNA. Translation: AAR12579.1. AK039249 mRNA. Translation: BAC30292.1. AK162804 mRNA. Translation: BAE37063.1. AK166310 mRNA. Translation: BAE38696.1. CH466619 Genomic DNA. Translation: EDL02097.1. CH466619 Genomic DNA. Translation: EDL02099.1. BC113201 mRNA. Translation: AAI13202.1.
IPI	IPI00468960. IPI00621783. IPI00830614. IPI00831191.
RefSeq	NP_035996.2. NM_011866.2.
UniGene	Mm.87161.
3D structure databases
ProteinModelPortal	Q8CA95.
SMR	Q8CA95. Positions 159-761.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8CA95. 1 interaction.
PTM databases
PhosphoSite	Q8CA95.
Proteomic databases
PaxDb	Q8CA95.
PRIDE	Q8CA95.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000089085; ENSMUSP00000086485; ENSMUSG00000023868. ENSMUST00000115720; ENSMUSP00000111385; ENSMUSG00000023868. ENSMUST00000115724; ENSMUSP00000111389; ENSMUSG00000023868. ENSMUST00000149440; ENSMUSP00000123216; ENSMUSG00000023868.
GeneID	23984.
KEGG	mmu:23984.
UCSC	uc008ajr.1. mouse. uc008ajs.1. mouse. uc008aju.1. mouse.
Organism-specific databases
CTD	10846.
MGI	MGI:1345143. Pde10a.
Phylogenomic databases
eggNOG	NOG270709.
GeneTree	ENSGT00550000074280.
HOGENOM	HOG000007068.
HOVERGEN	HBG082113.
InParanoid	Q3TLU6.
KO	K01120.
OMA	MVHRSCG.
Enzyme and pathway databases
UniPathway	UPA00762; UER00747. UPA00763; UER00748.
Gene expression databases
ArrayExpress	Q8CA95.
Bgee	Q8CA95.
Genevestigator	Q8CA95.
Family and domain databases
Gene3D	1.10.1300.10. 1 hit.
InterPro	IPR003018. GAF. IPR003607. HD/PDEase_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view]
Pfam	PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00065. GAF. 2 hits. SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1795126.
ChiTaRS	PDE10A. mouse.
NextBio	303873.
SOURCE	Search...

Entry information

Entry name

PDE10_MOUSE

Accession

Primary (citable) accession number: Q8CA95
Secondary accession number(s): Q3TLU6 , Q3TRG6, Q69C21, Q9WVI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	December 16, 2008
Last modified:	May 29, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program