Q8TCT7 (SPP2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal peptide peptidase-like 2B
Short name=SPP-like 2B
Short name=SPPL2b
EC=3.4.23.-

Alternative name(s):
Intramembrane protease 4
Short name=IMP-4
Presenilin homologous protein 4
Short name=PSH4
Presenilin-like protein 1

Gene names

Name:	SPPL2B
Synonyms:	IMP4, KIAA1532, PSL1

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	592 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	Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing. Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus. May play a role in the regulation of innate and adaptive immunity. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Subunit structure	Monomer. Homodimer. Interacts with ITM2B and TNF. Ref.11 Ref.13 Ref.14
Subcellular location	Golgi apparatus membrane; Multi-pass membrane protein. Note: targeted through the entire secretory pathway to endosomes/lysosomes. Ref.10 Ref.14
Tissue specificity	Expressed predominantly in adrenal cortex and mammary gland. Ref.9
Domain	The PAL motif is required for normal active site conformation By similarity. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family; therefore, it is predicted to cleave type II-oriented substrate peptides like the prototypic protease SPP.
Post-translational modification	Glycosylated. Ref.9 Ref.10
Sequence similarities	Belongs to the peptidase A22B family. Contains 1 PA (protease associated) domain.
Sequence caution	The sequence AAC05601.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAG45441.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAA96056.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	membrane protein ectodomain proteolysis Inferred from direct assay Ref.13Ref.14. Source: UniProtKB membrane protein intracellular domain proteolysis Inferred from direct assay Ref.13Ref.15. Source: UniProtKB regulation of immune response Inferred from mutant phenotype Ref.12. Source: UniProtKB
Cellular_component	Golgi-associated vesicle membrane Inferred from direct assay Ref.14. Source: UniProtKB endosome membrane Inferred from direct assay Ref.10. Source: UniProtKB integral to cytosolic side of endoplasmic reticulum membrane Inferred from direct assay Ref.9. Source: UniProtKB integral to lumenal side of endoplasmic reticulum membrane Inferred from direct assay Ref.9. Source: UniProtKB lysosomal membrane Inferred from direct assay Ref.10. Source: UniProtKB plasma membrane Inferred from direct assay Ref.12Ref.15. Source: UniProtKB
Molecular_function	aspartic endopeptidase activity, intramembrane cleaving Inferred from mutant phenotype Ref.15Ref.16. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.9Ref.10Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q8TCT7-1)

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: Q8TCT7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     320-592: Missing.

Isoform 3 (identifier: Q8TCT7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     280-291: Missing.
     320-592: Missing.

Isoform 4 (identifier: Q8TCT7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     506-511: KVLPPS → VNTSLL
     512-592: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 592	567	Signal peptide peptidase-like 2B		PRO_0000073909
Regions
	Topological domain	26 – 174	149	Lumenal Potential
	Transmembrane	175 – 195	21	Helical; Potential
	Topological domain	196 – 221	26	Cytoplasmic Potential
	Transmembrane	222 – 244	23	Helical; Potential
	Topological domain	245 – 248	4	Lumenal Potential
	Transmembrane	249 – 271	23	Helical; Potential
	Topological domain	272 – 293	22	Cytoplasmic Potential
	Transmembrane	294 – 314	21	Helical; Potential
	Topological domain	315 – 319	5	Lumenal Potential
	Transmembrane	320 – 340	21	Helical; Potential
	Topological domain	341 – 348	8	Cytoplasmic Potential
	Transmembrane	349 – 369	21	Helical; Potential
	Topological domain	370 – 412	43	Lumenal Potential
	Transmembrane	413 – 433	21	Helical; Potential
	Topological domain	434 – 445	12	Cytoplasmic Potential
	Transmembrane	446 – 466	21	Helical; Potential
	Topological domain	467 – 470	4	Lumenal Potential
	Transmembrane	471 – 491	21	Helical; Potential
	Topological domain	492 – 592	101	Cytoplasmic Potential
	Domain	71 – 149	79	PA
	Motif	472 – 474	3	PAL
	Compositional bias	350 – 357	8	Poly-Leu
	Compositional bias	509 – 551	43	Pro-rich
Sites
	Active site	359	1	By similarity
	Active site	421	1	By similarity
Amino acid modifications
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	129	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	280 – 291	12	Missing in isoform 3.		VSP_005203
	Alternative sequence	320 – 592	273	Missing in isoform 2 and isoform 3.		VSP_005204
	Alternative sequence	506 – 511	6	KVLPPS → VNTSLL in isoform 4.		VSP_009221
	Alternative sequence	512 – 592	81	Missing in isoform 4.		VSP_009222
	Natural variant	574	1	S → P. Corresponds to variant rs10402284 [ dbSNP | Ensembl ].		VAR_059780
Experimental info
	Mutagenesis	421	1	D → A: Loss of intramembrane-cleaving activity toward ITM2B and TNF. Ref.13 Ref.14 Ref.15 Ref.16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 16, 2006. Version 2. Checksum: 0F49370F16D36AA0	FASTA	592	64,644
	10 20 30 40 50 60 MAAAVAAALA RLLAAFLLLA AQVACEYGMV HVVSQAGGPE GKDYCILYNP QWAHLPHDLS 70 80 90 100 110 120 KASFLQLRNW TASLLCSAAD LPARGFSNQI PLVARGNCTF YEKVRLAQGS GARGLLIVSR 130 140 150 160 170 180 ERLVPPGGNK TQYDEIGIPV ALLSYKDMLD IFTRFGRTVR AALYAPKEPV LDYNMVIIFI 190 200 210 220 230 240 MAVGTVAIGG YWAGSRDVKK RYMKHKRDDG PEKQEDEAVD VTPVMTCVFV VMCCSMLVLL 250 260 270 280 290 300 YYFYDLLVYV VIGIFCLASA TGLYSCLAPC VRRLPFGKCR IPNNSLPYFH KRPQARMLLL 310 320 330 340 350 360 ALFCVAVSVV WGVFRNEDQW AWVLQDALGI AFCLYMLKTI RLPTFKACTL LLLVLFLYDI 370 380 390 400 410 420 FFVFITPFLT KSGSSIMVEV ATGPSDSATR EKLPMVLKVP RLNSSPLALC DRPFSLLGFG 430 440 450 460 470 480 DILVPGLLVA YCHRFDIQVQ SSRVYFVACT IAYGVGLLVT FVALALMQRG QPALLYLVPC 490 500 510 520 530 540 TLVTSCAVAL WRRELGVFWT GSGFAKVLPP SPWAPAPADG PQPPKDSATP LSPQPPSEEP 550 560 570 580 590 ATSPWPAEQS PKSRTSEEMG AGAPMREPGS PAESEGRDQA QPSPVTQPGA SA
	Isoform 2 [UniParc]. Checksum: 5EFEEB110C4C7D7B	FASTA	319	35,295
	10 20 30 40 50 60 MAAAVAAALA RLLAAFLLLA AQVACEYGMV HVVSQAGGPE GKDYCILYNP QWAHLPHDLS 70 80 90 100 110 120 KASFLQLRNW TASLLCSAAD LPARGFSNQI PLVARGNCTF YEKVRLAQGS GARGLLIVSR 130 140 150 160 170 180 ERLVPPGGNK TQYDEIGIPV ALLSYKDMLD IFTRFGRTVR AALYAPKEPV LDYNMVIIFI 190 200 210 220 230 240 MAVGTVAIGG YWAGSRDVKK RYMKHKRDDG PEKQEDEAVD VTPVMTCVFV VMCCSMLVLL 250 260 270 280 290 300 YYFYDLLVYV VIGIFCLASA TGLYSCLAPC VRRLPFGKCR IPNNSLPYFH KRPQARMLLL 310 ALFCVAVSVV WGVFRNEDQ
	Isoform 3 [UniParc]. Checksum: 4AFCE5838F23543F	FASTA	307	33,827
	10 20 30 40 50 60 MAAAVAAALA RLLAAFLLLA AQVACEYGMV HVVSQAGGPE GKDYCILYNP QWAHLPHDLS 70 80 90 100 110 120 KASFLQLRNW TASLLCSAAD LPARGFSNQI PLVARGNCTF YEKVRLAQGS GARGLLIVSR 130 140 150 160 170 180 ERLVPPGGNK TQYDEIGIPV ALLSYKDMLD IFTRFGRTVR AALYAPKEPV LDYNMVIIFI 190 200 210 220 230 240 MAVGTVAIGG YWAGSRDVKK RYMKHKRDDG PEKQEDEAVD VTPVMTCVFV VMCCSMLVLL 250 260 270 280 290 300 YYFYDLLVYV VIGIFCLASA TGLYSCLAPC VRRLPFGKCR PQARMLLLAL FCVAVSVVWG VFRNEDQ
	Isoform 4 [UniParc]. Checksum: 6B496A9879E9D57F	FASTA	511	56,431
	10 20 30 40 50 60 MAAAVAAALA RLLAAFLLLA AQVACEYGMV HVVSQAGGPE GKDYCILYNP QWAHLPHDLS 70 80 90 100 110 120 KASFLQLRNW TASLLCSAAD LPARGFSNQI PLVARGNCTF YEKVRLAQGS GARGLLIVSR 130 140 150 160 170 180 ERLVPPGGNK TQYDEIGIPV ALLSYKDMLD IFTRFGRTVR AALYAPKEPV LDYNMVIIFI 190 200 210 220 230 240 MAVGTVAIGG YWAGSRDVKK RYMKHKRDDG PEKQEDEAVD VTPVMTCVFV VMCCSMLVLL 250 260 270 280 290 300 YYFYDLLVYV VIGIFCLASA TGLYSCLAPC VRRLPFGKCR IPNNSLPYFH KRPQARMLLL 310 320 330 340 350 360 ALFCVAVSVV WGVFRNEDQW AWVLQDALGI AFCLYMLKTI RLPTFKACTL LLLVLFLYDI 370 380 390 400 410 420 FFVFITPFLT KSGSSIMVEV ATGPSDSATR EKLPMVLKVP RLNSSPLALC DRPFSLLGFG 430 440 450 460 470 480 DILVPGLLVA YCHRFDIQVQ SSRVYFVACT IAYGVGLLVT FVALALMQRG QPALLYLVPC 490 500 510 TLVTSCAVAL WRRELGVFWT GSGFAVNTSL L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a new protein family with homology to presenilins." Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	Martoglio B. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Novel class of polytopic proteins with domains associated with putative protease activity." Grigorenko A.P., Moliaka Y.K., Korovaitseva G.I., Rogaev E.I. Biokhimiia 67:826-834(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Blood.
[4]	"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"The DNA sequence and biology of human chromosome 19." 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. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 1; 2 AND 4). Tissue: Brain, Eye and Testis.
[8]	The European IMAGE consortium Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-318 (ISOFORM 3).
[9]	"Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins." Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U., Rovelli G., Martoglio B. J. Biol. Chem. 279:50790-50798(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION, TOPOLOGY, TISSUE SPECIFICITY.
[10]	"Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3." Krawitz P., Haffner C., Fluhrer R., Steiner H., Schmid B., Haass C. J. Biol. Chem. 280:39515-39523(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
[11]	"Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase." Nyborg A.C., Ladd T.B., Jansen K., Kukar T., Golde T.E. FASEB J. 20:1671-1679(2006) [PubMed] [Europe PMC] [Abstract] Cited for: HOMODIMERIZATION.
[12]	"SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production." Friedmann E., Hauben E., Maylandt K., Schleeger S., Vreugde S., Lichtenthaler S.F., Kuhn P.H., Stauffer D., Rovelli G., Martoglio B. Nat. Cell Biol. 8:843-848(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLEAVAGE OF TNF.
[13]	"A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b." Fluhrer R., Grammer G., Israel L., Condron M.M., Haffner C., Friedmann E., Bohland C., Imhof A., Martoglio B., Teplow D.B., Haass C. Nat. Cell Biol. 8:894-896(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLEAVAGE OF TNF, INTERACTION WITH TNF, MUTAGENESIS OF ASP-421.
[14]	"Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b." Martin L., Fluhrer R., Reiss K., Kremmer E., Saftig P., Haass C. J. Biol. Chem. 283:1644-1652(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLEAVAGE OF ITM2B, SUBCELLULAR LOCATION, INTERACTION WITH ITM2B, MUTAGENESIS OF ASP-421.
[15]	"Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysis." Martin L., Fluhrer R., Haass C. J. Biol. Chem. 284:5662-5670(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLEAVAGE OF ITM2B, MUTAGENESIS OF ASP-421.
[16]	"The alpha-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b)." Fluhrer R., Martin L., Klier B., Haug-Kroper M., Grammer G., Nuscher B., Haass C. J. Biol. Chem. 287:5156-5163(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CLEAVAGE OF ITM2B, MUTAGENESIS OF ASP-421.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ345027 mRNA. Translation: CAC87788.1. AJ420897 mRNA. Translation: CAD13134.1. AY169315 mRNA. Translation: AAO12540.1. AB040965 mRNA. Translation: BAA96056.1. Different initiation. AC004410 Genomic DNA. Translation: AAC05601.1. Sequence problems. AC005258 Genomic DNA. Translation: AAG45441.1. Different initiation. CH471139 Genomic DNA. Translation: EAW69383.1. CH471139 Genomic DNA. Translation: EAW69388.1. BC001788 mRNA. Translation: AAH01788.2. BC028391 mRNA. Translation: AAH28391.2. BC093046 mRNA. Translation: AAH93046.1. AL365405 mRNA. Translation: CAB96951.1. Sequence problems.
IPI	IPI00220530. IPI00304345. IPI00386494. IPI00398574.
RefSeq	NP_001070706.1. NM_001077238.1. NP_694533.1. NM_152988.2.
UniGene	Hs.744026.
3D structure databases
ProteinModelPortal	Q8TCT7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TCT7. 1 interaction.
Protein family/group databases
MEROPS	A22.004.
PTM databases
PhosphoSite	Q8TCT7.
Polymorphism databases
DMDM	97537015.
Proteomic databases
PaxDb	Q8TCT7.
PRIDE	Q8TCT7.
Protocols and materials databases
DNASU	56928.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	56928.
KEGG	hsa:56928.
UCSC	uc002lvr.3. human. uc002lvs.3. human.
Organism-specific databases
CTD	56928.
GeneCards	GC19P002328.
H-InvDB	HIX0158528.
HGNC	HGNC:30627. SPPL2B.
MIM	608239. gene.
neXtProt	NX_Q8TCT7.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG250196.
HOVERGEN	HBG024193.
InParanoid	Q8TCT7.
KO	K09597.
OrthoDB	EOG4Q2DF6.
Gene expression databases
Genevestigator	Q8TCT7.
GermOnline	ENSG00000005206. Homo sapiens.
Family and domain databases
InterPro	IPR006639. Peptidase_A22. IPR007369. Peptidase_A22B_SPP. IPR003137. Protease-assoc_domain. [Graphical view]
PANTHER	PTHR12174. PTHR12174. 1 hit.
Pfam	PF02225. PA. 1 hit. PF04258. Peptidase_A22B. 1 hit. [Graphical view]
SMART	SM00730. PSN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SPPL2B. human.
GenomeRNAi	56928.
NextBio	62462.
SOURCE	Search...

Entry information

Entry name

SPP2B_HUMAN

Accession

Primary (citable) accession number: Q8TCT7
Secondary accession number(s): D6W609 , O60365, Q567S3, Q8IUH9, Q9BUY6, Q9H3M4, Q9NPN2, Q9P1Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	May 16, 2006
Last modified:	May 29, 2013
This is version 107 of the entry and version 2 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.