P08697 (A2AP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-2-antiplasmin
Short name=Alpha-2-AP

Alternative name(s):
Alpha-2-plasmin inhibitor
Short name=Alpha-2-PI
Serpin F2

Gene names

Name:	SERPINF2
Synonyms:	AAP, PLI

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	491 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	Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin. Ref.16
Subunit structure	Forms protease inhibiting heterodimer with TMPRSS7.
Subcellular location	Secreted.
Tissue specificity	Expressed by the liver and secreted in plasma.
Involvement in disease	Alpha-2-plasmin inhibitor deficiency (APLID) [MIM:262850]: An autosomal recessive disorder resulting in severe hemorrhagic diathesis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19
Sequence similarities	Belongs to the serpin family.

Ontologies

Keywords
Biological process	Acute phase
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein Isopeptide bond Sulfation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW blood vessel morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL collagen fibril organization Inferred from sequence or structural similarity PubMed 17958745. Source: BHF-UCL fibrinolysis Traceable author statement. Source: Reactome negative regulation of fibrinolysis Inferred from direct assay PubMed 134998. Source: BHF-UCL negative regulation of plasminogen activation Inferred from direct assay PubMed 134998. Source: BHF-UCL platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of ERK1 and ERK2 cascade Inferred from direct assay PubMed 20008146. Source: BHF-UCL positive regulation of JNK cascade Inferred from direct assay PubMed 20008146. Source: BHF-UCL positive regulation of cell differentiation Inferred from direct assay PubMed 20008146. Source: BHF-UCL positive regulation of cell-cell adhesion mediated by cadherin Traceable author statement PubMed 17203182. Source: BHF-UCL positive regulation of collagen biosynthetic process Inferred from direct assay PubMed 17958745. Source: BHF-UCL positive regulation of smooth muscle cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of stress fiber assembly Inferred from direct assay PubMed 20008146. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 17958745. Source: BHF-UCL positive regulation of transforming growth factor beta production Inferred from direct assay PubMed 17958745PubMed 20008146. Source: BHF-UCL regulation of blood vessel size by renin-angiotensin Inferred from sequence or structural similarity. Source: BHF-UCL regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome response to organic substance Inferred from electronic annotation. Source: Compara
Cellular_component	fibrinogen complex Inferred from direct assay PubMed 17317851. Source: BHF-UCL platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	eukaryotic cell surface binding Inferred from direct assay PubMed 17958745. Source: BHF-UCL serine-type endopeptidase inhibitor activity Non-traceable author statement PubMed 12878203. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P08697-1)

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: P08697-2)

The sequence of this isoform differs from the canonical sequence as follows:
     56-119: Missing.
     120-122: LAL → VQP

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Ref.8 Ref.9
	Propeptide	28 – 39	12			PRO_0000032511
	Chain	40 – 491	452	Alpha-2-antiplasmin		PRO_0000032512
Sites
	Site	403 – 404	2	Reactive bond for plasmin
	Site	404 – 405	2	Reactive bond for chymotrypsin
Amino acid modifications
	Modified residue	484	1	Sulfotyrosine
	Glycosylation	126	1	N-linked (GlcNAc...) Ref.17
	Glycosylation	295	1	N-linked (GlcNAc...) Ref.17
	Glycosylation	309	1	N-linked (GlcNAc...) Ref.17
	Glycosylation	316	1	N-linked (GlcNAc...) Potential
	Disulfide bond	70 ↔ 143		Ref.15
	Cross-link	41		Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-322 in alpha-fibrinogen)
Natural variations
	Alternative sequence	56 – 119	64	Missing in isoform 2.		VSP_043833
	Alternative sequence	120 – 122	3	LAL → VQP in isoform 2.		VSP_043834
	Natural variant	2	1	A → V. Ref.6 Corresponds to variant rs2070862 [ dbSNP | Ensembl ].		VAR_047951
	Natural variant	27	1	A → V. Ref.19		VAR_013252
	Natural variant	33	1	R → W. Ref.19 Corresponds to variant rs2070863 [ dbSNP | Ensembl ].		VAR_013253
	Natural variant	98	1	A → G. Corresponds to variant rs36021516 [ dbSNP | Ensembl ].		VAR_051956
	Natural variant	176	1	Missing in APLID; variant Okinawa; probably blocks intracellular transport of alpha-2-plasmin inhibitor. Ref.18		VAR_013254
	Natural variant	411	1	V → M in APLID. Ref.19		VAR_013255
	Natural variant	434	1	R → K. Ref.19 Corresponds to variant rs1057335 [ dbSNP | Ensembl ].		VAR_013256
	Natural variant	451	1	P → S. Corresponds to variant rs57360598 [ dbSNP | Ensembl ].		VAR_061792
Experimental info
	Sequence conflict	49	1	L → G AA sequence Ref.10
	Sequence conflict	105	1	N → D AA sequence Ref.10
	Sequence conflict	289	1	H → D in AAA35543. Ref.7
	Sequence conflict	408	1	S → G AA sequence Ref.10
	Sequence conflict	455	1	D → N AA sequence Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1990. Version 3. Checksum: 385A1C90E91A63CB	FASTA	491	54,566
	10 20 30 40 50 60 MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL KLGNQEPGGQ 70 80 90 100 110 120 TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL 130 140 150 160 170 180 ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE 190 200 210 220 230 240 QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF 250 260 270 280 290 300 WRNKFDPSLT QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV 310 320 330 340 350 360 LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF 370 380 390 400 410 420 QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF 430 440 450 460 470 480 EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM 490 EEDYPQFGSP K
	Isoform 2 [UniParc]. Checksum: 1A5190EC32B5350A	FASTA	427	47,907
	10 20 30 40 50 60 MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL KLGNQVQPGA 70 80 90 100 110 120 QNHTLQRLQQ VLHAGSGPCL PHLLSRLCQD LGPGAFRLAA RMYLQKGFPI KEDFLEQSEQ 130 140 150 160 170 180 LFGAKPVSLT GKQEDDLANI NQWVKEATEG KIQEFLSGLP EDTVLLLLNA IHFQGFWRNK 190 200 210 220 230 240 FDPSLTQRDS FHLDEQFTVP VEMMQARTYP LRWFLLEQPE IQVAHFPFKN NMSFVVLVPT 250 260 270 280 290 300 HFEWNVSQVL ANLSWDTLHP PLVWERPTKV RLPKLYLKHQ MDLVATLSQL GLQELFQAPD 310 320 330 340 350 360 LRGISEQSLV VSGVQHQSTL ELSEVGVEAA AATSIAMSRM SLSSFSVNRP FLFFIFEDTT 370 380 390 400 410 420 GLPLFVGSVR NPNPSAPREL KEQQDSPGNK DFLQSLKGFP RGDKLFGPDL KLVPPMEEDY PQFGSPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence." Tone M., Kikuno R., Kume-Iwaki A., Hashimoto-Gotoh T. J. Biochem. 102:1033-1041(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"Organization of the human alpha 2-plasmin inhibitor gene." Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N. Proc. Natl. Acad. Sci. U.S.A. 85:6836-6840(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
[3]	Erratum Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N. Proc. Natl. Acad. Sci. U.S.A. 86:1612-1613(1989)
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Liver.
[5]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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), VARIANT VAL-2.
[7]	"Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin)." Holmes W.E., Nelles L., Lijnen H.R., Collen D. J. Biol. Chem. 262:1659-1664(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-491 (ISOFORM 1).
[8]	"Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma." Bangert K., Johnsen A.H., Christensen U., Thorsen S. Biochem. J. 291:623-625(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-58. Tissue: Plasma.
[9]	"Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence." Christensen S., Sottrup-Jensen L. FEBS Lett. 312:100-104(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-52. Tissue: Plasma.
[10]	"Amino-acid sequence of human alpha 2-antiplasmin." Lijnen H.R., Holmes W.E., van Hoef B., Wiman B., Rodriguez H., Collen D. Eur. J. Biochem. 166:565-574(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-491.
[11]	"Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma." Wiman B., Collen D. Eur. J. Biochem. 78:19-26(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-43.
[12]	"Structure of the carboxyl-terminal half of human alpha 2-plasmin inhibitor deduced from that of cDNA." Sumi Y., Nakamura Y., Aoki N., Sakai M., Muramatsu M. J. Biochem. 100:1399-1402(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-491.
[13]	"Sulfation of a tyrosine residue in the plasmin-binding domain of alpha 2-antiplasmin." Hortin G., Fok K.F., Toren P.C., Strauss A.W. J. Biol. Chem. 262:3082-3085(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 481-491, SULFATION.
[14]	"Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive sites." Potempa J., Shieh B.-H., Travis J. Science 241:699-700(1988) [PubMed] [Europe PMC] [Abstract] Cited for: REACTIVE SITES.
[15]	"Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties." Christensen S., Valnickova Z., Thogersen I.B., Olsen E.H., Enghild J.J. Biochem. J. 323:847-852(1997) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BOND.
[16]	"Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity." Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H. Biochem. J. 390:231-242(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, HETERODIMER WITH TMPRSS7.
[17]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-295 AND ASN-309, MASS SPECTROMETRY. Tissue: Plasma.
[18]	"Hereditary alpha 2-plasmin inhibitor deficiency caused by a transport-deficient mutation (alpha 2-PI-Okinawa). Deletion of Glu137 by a trinucleotide deletion blocks intracellular transport." Miura O., Sugahara Y., Aoki N. J. Biol. Chem. 264:18213-18219(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT APLID GLU-176 DEL.
[19]	"A novel missense mutation in the human plasmin inhibitor (alpha2-antiplasmin) gene associated with a bleeding tendency." Lind B., Thorsen S. Br. J. Haematol. 107:317-322(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT APLID MET-411, VARIANTS VAL-27; TRP-33 AND LYS-434.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00174 mRNA. Translation: BAA00124.1. M20786 , M20782, M20783, M20784, M20785 Genomic DNA. Translation: AAA51554.1. AK303763 mRNA. Translation: BAG64729.1. AC130343 Genomic DNA. No translation available. BC031592 mRNA. Translation: AAH31592.1. J02654 mRNA. Translation: AAA35543.1. D00116 mRNA. Translation: BAA00070.1.
IPI	IPI00879231.
PIR	ITHUA2. A31402.
RefSeq	NP_000925.2. NM_000934.3. NP_001159392.1. NM_001165920.1. NP_001159393.1. NM_001165921.1.
UniGene	Hs.159509.
3D structure databases
ProteinModelPortal	P08697.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08697. 2 interactions.
STRING	9606.ENSP00000321853.
Protein family/group databases
MEROPS	I04.023.
PTM databases
PhosphoSite	P08697.
Polymorphism databases
DMDM	112907.
2D gel databases
SWISS-2DPAGE	P08697.
Proteomic databases
PaxDb	P08697.
PRIDE	P08697.
Protocols and materials databases
DNASU	5345.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324015; ENSP00000321853; ENSG00000167711. ENST00000382061; ENSP00000371493; ENSG00000167711. ENST00000450523; ENSP00000403877; ENSG00000167711.
GeneID	5345.
KEGG	hsa:5345.
UCSC	uc002ftk.1. human.
Organism-specific databases
CTD	5345.
GeneCards	GC17P001593.
H-InvDB	HIX0013407.
HGNC	HGNC:9075. SERPINF2.
HPA	CAB024863. HPA001885.
MIM	262850. phenotype. 613168. gene.
neXtProt	NX_P08697.
Orphanet	79. Congenital alpha2 antiplasmin deficiency.
PharmGKB	PA35522.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4826.
HOGENOM	HOG000231761.
HOVERGEN	HBG000043.
InParanoid	P08697.
KO	K03983.
OMA	RDSFHLD.
PhylomeDB	P08697.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P08697.
Bgee	P08697.
CleanEx	HS_SERPINF2.
Genevestigator	P08697.
Family and domain databases
InterPro	IPR023795. Protease_inhib_I4_serpin_CS. IPR023796. Serpin_dom. IPR000215. Serpin_fam. [Graphical view]
PANTHER	PTHR11461. PTHR11461. 1 hit.
Pfam	PF00079. Serpin. 1 hit. [Graphical view]
SMART	SM00093. SERPIN. 1 hit. [Graphical view]
SUPFAM	SSF56574. Prot_inh_serpin. 1 hit.
PROSITE	PS00284. SERPIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SERPINF2. human.
DrugBank	DB00086. Streptokinase.
GenomeRNAi	5345.
NextBio	20714.
PMAP-CutDB	P08697.
SOURCE	Search...

Entry information

Entry name

A2AP_HUMAN

Accession

Primary (citable) accession number: P08697
Secondary accession number(s): B4E1B7 , Q8N5U7, Q9UCG2, Q9UCG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 148 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.