Q9UIQ6 (LCAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leucyl-cystinyl aminopeptidase
Short name=Cystinyl aminopeptidase
EC=3.4.11.3

Alternative name(s):
Insulin-regulated membrane aminopeptidase
Insulin-responsive aminopeptidase
Short name=IRAP
Oxytocinase
Short name=OTase
Placental leucine aminopeptidase
Short name=P-LAP

Cleaved into the following chain:

1. Leucyl-cystinyl aminopeptidase, pregnancy serum form

Gene names

Name:	LNPEP
Synonyms:	OTASE

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	1025 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	Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain. Ref.4 Ref.7 Ref.8
Catalytic activity	Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however. Ref.4 Ref.7
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer. Binds tankyrases 1 and 2.
Subcellular location	Cell membrane; Single-pass type II membrane protein. Note: In brain only the membrane-bound form is found. The protein resides in intracellular vesicles together with GLUT4 and can then translocate to the cell surface in response to insulin and/or oxytocin. Localization may be determined by dileucine internalization motifs, and/or by interaction with tankyrases. Ref.4 Leucyl-cystinyl aminopeptidase, pregnancy serum form: Secreted. Note: During pregnancy serum levels are low in the first trimester, rise progressively during the second and third trimester and decrease rapidly after parturition. Ref.4
Tissue specificity	Highly expressed in placenta, heart, kidney and small intestine. Detected at lower levels in neuronal cells in the brain, in skeletal muscle, spleen, liver, testes and colon. Ref.1 Ref.2 Ref.4
Post-translational modification	The pregnancy serum form is derived from the membrane-bound form by proteolytic processing. N-glycosylated.
Sequence similarities	Belongs to the peptidase M1 family.
Sequence caution	The sequence BAA09436.1 differs from that shown. Reason: Erroneous initiation. The sequence BAD92120.1 differs from that shown. Reason: Frameshift at position 405.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Traceable author statement. Source: Reactome cell-cell signaling Traceable author statement Ref.1. Source: ProtInc female pregnancy Traceable author statement Ref.1. Source: ProtInc protein catabolic process Inferred from electronic annotation. Source: Compara protein polyubiquitination Traceable author statement. Source: Reactome proteolysis Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome early endosome lumen Traceable author statement. Source: Reactome extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	aminopeptidase activity Traceable author statement PubMed 15691326. Source: HGNC metallopeptidase activity Traceable author statement Ref.2. Source: ProtInc zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

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

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9UIQ6-1)

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: Q9UIQ6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.

Isoform 3 (identifier: Q9UIQ6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1025	1025	Leucyl-cystinyl aminopeptidase		PRO_0000095114
	Chain	155 – 1025	871	Leucyl-cystinyl aminopeptidase, pregnancy serum form		PRO_0000292264
Regions
	Topological domain	1 – 110	110	Cytoplasmic Potential
	Transmembrane	111 – 131	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	132 – 1025	894	Extracellular Potential
	Region	96 – 101	6	Tankyrase binding
	Region	428 – 432	5	Substrate binding By similarity
	Motif	53 – 54	2	Dileucine internalization motif Potential
	Motif	76 – 77	2	Dileucine internalization motif Potential
Sites
	Active site	465	1	Proton acceptor By similarity
	Metal binding	464	1	Zinc; catalytic By similarity
	Metal binding	468	1	Zinc; catalytic By similarity
	Metal binding	487	1	Zinc; catalytic By similarity
	Binding site	295	1	Substrate By similarity
	Site	154 – 155	2	Cleavage; to produce pregnancy serum form
	Site	549	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	80	1	Phosphoserine By similarity
	Modified residue	91	1	Phosphoserine By similarity
	Glycosylation	145	1	N-linked (GlcNAc...) Potential
	Glycosylation	184	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	215	1	N-linked (GlcNAc...) Potential
	Glycosylation	256	1	N-linked (GlcNAc...) Potential
	Glycosylation	266	1	N-linked (GlcNAc...) Potential
	Glycosylation	368	1	N-linked (GlcNAc...) Potential
	Glycosylation	374	1	N-linked (GlcNAc...) Potential
	Glycosylation	448	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	525	1	N-linked (GlcNAc...) Potential
	Glycosylation	578	1	N-linked (GlcNAc...) Potential
	Glycosylation	598	1	N-linked (GlcNAc...) Potential
	Glycosylation	664	1	N-linked (GlcNAc...) Potential
	Glycosylation	682	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	760	1	N-linked (GlcNAc...) Potential
	Glycosylation	834	1	N-linked (GlcNAc...) Potential
	Glycosylation	850	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	989	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 19	19	Missing in isoform 3.		VSP_005449
	Alternative sequence	1 – 14	14	Missing in isoform 2.		VSP_005448
	Natural variant	86	1	S → P. Corresponds to variant rs3797799 [ dbSNP | Ensembl ].		VAR_031616
	Natural variant	594	1	N → I. Corresponds to variant rs12520455 [ dbSNP | Ensembl ].		VAR_051567
	Natural variant	763	1	A → T. Corresponds to variant rs2303138 [ dbSNP | Ensembl ].		VAR_012812
	Natural variant	913	1	S → T. Corresponds to variant rs17087233 [ dbSNP | Ensembl ].		VAR_051568
	Natural variant	963	1	I → V. Corresponds to variant rs11746232 [ dbSNP | Ensembl ].		VAR_031617
Experimental info
	Sequence conflict	66	1	D → V in CAB61646. Ref.3
	Sequence conflict	66	1	D → V in CAB94753. Ref.3
	Sequence conflict	301	1	S → L AA sequence Ref.6
	Sequence conflict	386	1	K → N in AAB66672. Ref.2
	Sequence conflict	386	1	K → N in AAB66673. Ref.2
	Sequence conflict	386	1	K → N in CAB61646. Ref.3
	Sequence conflict	386	1	K → N in CAB94753. Ref.3
	Sequence conflict	892	1	K → Q in BAA09436. Ref.1
	Sequence conflict	944	1	F → L in BAA09436. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 17, 2007. Version 3. Checksum: F84C0EA9D48DC2C0	FASTA	1,025	117,349
	10 20 30 40 50 60 MEPFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE 70 80 90 100 110 120 HEMEEDEEDY ESSAKLLGMS FMNRSSGLRN SATGYRQSPD GACSVPSART MVVCAFVIVV 130 140 150 160 170 180 AVSVIMVIYL LPRCTFTKEG CHKKNQSIGL IQPFATNGKL FPWAQIRLPT AVVPLRYELS 190 200 210 220 230 240 LHPNLTSMTF RGSVTISVQA LQVTWNIILH STGHNISRVT FMSAVSSQEK QAEILEYAYH 250 260 270 280 290 300 GQIAIVAPEA LLAGHNYTLK IEYSANISSS YYGFYGFSYT DESNEKKYFA ATQFEPLAAR 310 320 330 340 350 360 SAFPCFDEPA FKATFIIKII RDEQYTALSN MPKKSSVVLD DGLVQDEFSE SVKMSTYLVA 370 380 390 400 410 420 FIVGEMKNLS QDVNGTLVSI YAVPEKIGQV HYALETTVKL LEFFQNYFEI QYPLKKLDLV 430 440 450 460 470 480 AIPDFEAGAM ENWGLLTFRE ETLLYDSNTS SMADRKLVTK IIAHELAHQW FGNLVTMKWW 490 500 510 520 530 540 NDLWLNEGFA TFMEYFSLEK IFKELSSYED FLDARFKTMK KDSLNSSHPI SSSVQSSEQI 550 560 570 580 590 600 EEMFDSLSYF KGSSLLLMLK TYLSEDVFQH AVVLYLHNHS YASIQSDDLW DSFNEVTNQT 610 620 630 640 650 660 LDVKRMMKTW TLQKGFPLVT VQKKGKELFI QQERFFLNMK PEIQPSDTSY LWHIPLSYVT 670 680 690 700 710 720 EGRNYSKYQS VSLLDKKSGV INLTEEVLWV KVNINMNGYY IVHYADDDWE ALIHQLKINP 730 740 750 760 770 780 YVLSDKDRAN LINNIFELAG LGKVPLKRAF DLINYLGNEN HTAPITEALF QTDLIYNLLE 790 800 810 820 830 840 KLGYMDLASR LVTRVFKLLQ NQIQQQTWTD EGTPSMRELR SALLEFACTH NLGNCSTTAM 850 860 870 880 890 900 KLFDDWMASN GTQSLPTDVM TTVFKVGAKT DKGWSFLLGK YISIGSEAEK NKILEALASS 910 920 930 940 950 960 EDVRKLYWLM KSSLNGDNFR TQKLSFIIRT VGRHFPGHLL AWDFVKENWN KLVQKFPLGS 970 980 990 1000 1010 1020 YTIQNIVAGS TYLFSTKTHL SEVQAFFENQ SEATFRLRCV QEALEVIQLN IQWMEKNLKS LTWWL
	Isoform 2 [UniParc]. Checksum: FBB54EFECFBA8FD9	FASTA	1,011	115,636
	10 20 30 40 50 60 MIENSMFEEE PDVVDLAKEP CLHPLEPDEV EYEPRGSRLL VRGLGEHEME EDEEDYESSA 70 80 90 100 110 120 KLLGMSFMNR SSGLRNSATG YRQSPDGACS VPSARTMVVC AFVIVVAVSV IMVIYLLPRC 130 140 150 160 170 180 TFTKEGCHKK NQSIGLIQPF ATNGKLFPWA QIRLPTAVVP LRYELSLHPN LTSMTFRGSV 190 200 210 220 230 240 TISVQALQVT WNIILHSTGH NISRVTFMSA VSSQEKQAEI LEYAYHGQIA IVAPEALLAG 250 260 270 280 290 300 HNYTLKIEYS ANISSSYYGF YGFSYTDESN EKKYFAATQF EPLAARSAFP CFDEPAFKAT 310 320 330 340 350 360 FIIKIIRDEQ YTALSNMPKK SSVVLDDGLV QDEFSESVKM STYLVAFIVG EMKNLSQDVN 370 380 390 400 410 420 GTLVSIYAVP EKIGQVHYAL ETTVKLLEFF QNYFEIQYPL KKLDLVAIPD FEAGAMENWG 430 440 450 460 470 480 LLTFREETLL YDSNTSSMAD RKLVTKIIAH ELAHQWFGNL VTMKWWNDLW LNEGFATFME 490 500 510 520 530 540 YFSLEKIFKE LSSYEDFLDA RFKTMKKDSL NSSHPISSSV QSSEQIEEMF DSLSYFKGSS 550 560 570 580 590 600 LLLMLKTYLS EDVFQHAVVL YLHNHSYASI QSDDLWDSFN EVTNQTLDVK RMMKTWTLQK 610 620 630 640 650 660 GFPLVTVQKK GKELFIQQER FFLNMKPEIQ PSDTSYLWHI PLSYVTEGRN YSKYQSVSLL 670 680 690 700 710 720 DKKSGVINLT EEVLWVKVNI NMNGYYIVHY ADDDWEALIH QLKINPYVLS DKDRANLINN 730 740 750 760 770 780 IFELAGLGKV PLKRAFDLIN YLGNENHTAP ITEALFQTDL IYNLLEKLGY MDLASRLVTR 790 800 810 820 830 840 VFKLLQNQIQ QQTWTDEGTP SMRELRSALL EFACTHNLGN CSTTAMKLFD DWMASNGTQS 850 860 870 880 890 900 LPTDVMTTVF KVGAKTDKGW SFLLGKYISI GSEAEKNKIL EALASSEDVR KLYWLMKSSL 910 920 930 940 950 960 NGDNFRTQKL SFIIRTVGRH FPGHLLAWDF VKENWNKLVQ KFPLGSYTIQ NIVAGSTYLF 970 980 990 1000 1010 STKTHLSEVQ AFFENQSEAT FRLRCVQEAL EVIQLNIQWM EKNLKSLTWW L
	Isoform 3 [UniParc]. Checksum: F57E71F1AA3C28E3	FASTA	1,006	115,062
	10 20 30 40 50 60 MFEEEPDVVD LAKEPCLHPL EPDEVEYEPR GSRLLVRGLG EHEMEEDEED YESSAKLLGM 70 80 90 100 110 120 SFMNRSSGLR NSATGYRQSP DGACSVPSAR TMVVCAFVIV VAVSVIMVIY LLPRCTFTKE 130 140 150 160 170 180 GCHKKNQSIG LIQPFATNGK LFPWAQIRLP TAVVPLRYEL SLHPNLTSMT FRGSVTISVQ 190 200 210 220 230 240 ALQVTWNIIL HSTGHNISRV TFMSAVSSQE KQAEILEYAY HGQIAIVAPE ALLAGHNYTL 250 260 270 280 290 300 KIEYSANISS SYYGFYGFSY TDESNEKKYF AATQFEPLAA RSAFPCFDEP AFKATFIIKI 310 320 330 340 350 360 IRDEQYTALS NMPKKSSVVL DDGLVQDEFS ESVKMSTYLV AFIVGEMKNL SQDVNGTLVS 370 380 390 400 410 420 IYAVPEKIGQ VHYALETTVK LLEFFQNYFE IQYPLKKLDL VAIPDFEAGA MENWGLLTFR 430 440 450 460 470 480 EETLLYDSNT SSMADRKLVT KIIAHELAHQ WFGNLVTMKW WNDLWLNEGF ATFMEYFSLE 490 500 510 520 530 540 KIFKELSSYE DFLDARFKTM KKDSLNSSHP ISSSVQSSEQ IEEMFDSLSY FKGSSLLLML 550 560 570 580 590 600 KTYLSEDVFQ HAVVLYLHNH SYASIQSDDL WDSFNEVTNQ TLDVKRMMKT WTLQKGFPLV 610 620 630 640 650 660 TVQKKGKELF IQQERFFLNM KPEIQPSDTS YLWHIPLSYV TEGRNYSKYQ SVSLLDKKSG 670 680 690 700 710 720 VINLTEEVLW VKVNINMNGY YIVHYADDDW EALIHQLKIN PYVLSDKDRA NLINNIFELA 730 740 750 760 770 780 GLGKVPLKRA FDLINYLGNE NHTAPITEAL FQTDLIYNLL EKLGYMDLAS RLVTRVFKLL 790 800 810 820 830 840 QNQIQQQTWT DEGTPSMREL RSALLEFACT HNLGNCSTTA MKLFDDWMAS NGTQSLPTDV 850 860 870 880 890 900 MTTVFKVGAK TDKGWSFLLG KYISIGSEAE KNKILEALAS SEDVRKLYWL MKSSLNGDNF 910 920 930 940 950 960 RTQKLSFIIR TVGRHFPGHL LAWDFVKENW NKLVQKFPLG SYTIQNIVAG STYLFSTKTH 970 980 990 1000 LSEVQAFFEN QSEATFRLRC VQEALEVIQL NIQWMEKNLK SLTWWL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human placental leucine aminopeptidase/oxytocinase. A new member of type II membrane-spanning zinc metallopeptidase family." Rogi T., Tsujimoto M., Nakazato H., Mizutani S., Tomoda Y. J. Biol. Chem. 271:56-61(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 160-168; 319-332; 615-624; 635-647; 798-814 AND 870-880, TISSUE SPECIFICITY. Tissue: Placenta.
[2]	"The complete amino acid sequence of human placental oxytocinase." Laustsen P.G., Rasmussen T.E., Petersen K., Pedraza-Diaz S., Moestrup S.K., Gliemann J., Sottrup-Jensen L., Kristensen T. Biochim. Biophys. Acta 1352:1-7(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Tissue: Placenta.
[3]	"Structure of the human oxytocinase/insulin-regulated aminopeptidase gene and localization to chromosome 5q21." Rasmussen T.E., Pedraza-Diaz S., Hardre R., Laustsen P.G., Carrion A.G., Kristensen T. Eur. J. Biochem. 267:2297-2306(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
[4]	"Expression of placental leucine aminopeptidase/oxytocinase in neuronal cells and its action on neuronal peptides." Matsumoto H., Nagasaka T., Hattori A., Rogi T., Tsuruoka N., Mizutani S., Tsujimoto M. Eur. J. Biochem. 268:3259-3266(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 206-1025. Tissue: Brain.
[6]	"Pool sequencing of natural HLA-DR, DQ, and DP ligands reveals detailed peptide motifs, constraints of processing, and general rules." Falk K., Roetzschke O., Stevanovic S., Jung G., Rammensee H.G. Immunogenetics 39:230-242(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 285-301 AND 710-724.
[7]	"Identification of human placental leucine aminopeptidase as oxytocinase." Tsujimoto M., Mizutani S., Adachi H., Kimura M., Nakazato H., Tomoda Y. Arch. Biochem. Biophys. 292:388-392(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[8]	"Evidence that the angiotensin IV (AT(4)) receptor is the enzyme insulin-regulated aminopeptidase." Albiston A.L., McDowall S.G., Matsacos D., Sim P., Clune E., Mustafa T., Lee J., Mendelsohn F.A., Simpson R.J., Connolly L.M., Chai S.Y. J. Biol. Chem. 276:48623-48626(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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-184; ASN-448; ASN-682 AND ASN-850, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50810 mRNA. Translation: BAA09436.1. Different initiation. U62768 mRNA. Translation: AAB66672.1. U62769 mRNA. Translation: AAB66673.1. AJ131023 , AJ131025, AJ131026, AJ131027, AJ131028, AJ131029, AJ131030, AJ131031, AJ131032, AJ131033, AJ131034, AJ131035, AJ131036, AJ131037, AJ131038, AJ131039 Genomic DNA. Translation: CAB61646.1. AJ131025 , AJ131026, AJ131027, AJ131028, AJ131029, AJ131030, AJ131031, AJ131032, AJ131033, AJ131034, AJ131035, AJ131036, AJ131037, AJ131038, AJ131039 Genomic DNA. Translation: CAB94753.1. AB208883 mRNA. Translation: BAD92120.1. Frameshift.
IPI	IPI00221240. IPI00221241. IPI00307017.
PIR	A59383. A59384.
RefSeq	NP_005566.2. NM_005575.2. NP_787116.2. NM_175920.3.
UniGene	Hs.527199. Hs.656905.
3D structure databases
ProteinModelPortal	Q9UIQ6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UIQ6. 4 interactions.
STRING	9606.ENSP00000231368.
Protein family/group databases
MEROPS	M01.011.
PTM databases
PhosphoSite	Q9UIQ6.
Polymorphism databases
DMDM	145559489.
Proteomic databases
PaxDb	Q9UIQ6.
PeptideAtlas	Q9UIQ6.
PRIDE	Q9UIQ6.
Protocols and materials databases
DNASU	4012.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000231368; ENSP00000231368; ENSG00000113441. ENST00000395770; ENSP00000379117; ENSG00000113441.
GeneID	4012.
KEGG	hsa:4012.
UCSC	uc003kmv.1. human.
Organism-specific databases
CTD	4012.
GeneCards	GC05P096272.
H-InvDB	HIX0005054.
HGNC	HGNC:6656. LNPEP.
HPA	HPA043642.
MIM	151300. gene.
neXtProt	NX_Q9UIQ6.
PharmGKB	PA30418.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0308.
HOVERGEN	HBG108296.
InParanoid	Q9UIQ6.
KO	K01257.
OMA	VTFMSAV.
OrthoDB	EOG4HDSSX.
Enzyme and pathway databases
Pathway_Interaction_DB	insulin_glucose_pathway. Insulin-mediated glucose transport.
Reactome	REACT_11123. Membrane Trafficking. REACT_6900. Immune System.
Gene expression databases
Bgee	Q9UIQ6.
CleanEx	HS_LNPEP.
Genevestigator	Q9UIQ6.
GermOnline	ENSG00000113441. Homo sapiens.
Family and domain databases
InterPro	IPR024571. DUF3358. IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. PTHR11533. 1 hit.
Pfam	PF11838. DUF3358. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UIQ6.
ChEMBL	CHEMBL2693.
GenomeRNAi	4012.
NextBio	15736.
PMAP-CutDB	Q9UIQ6.
SOURCE	Search...

Entry information

Entry name

LCAP_HUMAN

Accession

Primary (citable) accession number: Q9UIQ6
Secondary accession number(s): O00769 , Q15145, Q59H76, Q9TNQ2, Q9TNQ3, Q9UIQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	April 17, 2007
Last modified:	May 1, 2013
This is version 129 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.