O95672 (ECEL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endothelin-converting enzyme-like 1
EC=3.4.24.-

Alternative name(s):
Xce protein

Gene names

Name:	ECEL1
Synonyms:	XCE
ORF Names:	UNQ2431/PRO4991

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	775 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May contribute to the degradation of peptide hormones and be involved in the inactivation of neuronal peptides.
Cofactor	Binds 1 zinc ion By similarity.
Subcellular location	Membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Highly expressed in the CNS, in particular in putamen, spinal cord, medulla and subthalamic nucleus. A strong signal was also detected in uterine subepithelial cells and around renal blood vessels. Detected at lower levels in amygdala, caudate, thalamus, pancreas and skeletal muscle. Detected at very low levels in substantia nigra, cerebellum, cortex, corpus callosum and hippocampus.
Post-translational modification	N-glycosylated.
Sequence similarities	Belongs to the peptidase M13 family.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	neuropeptide signaling pathway Traceable author statement Ref.1. Source: ProtInc proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: Compara metallopeptidase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: O95672-1)

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: O95672-2)

The sequence of this isoform differs from the canonical sequence as follows:
     561-562: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 775	775	Endothelin-converting enzyme-like 1		PRO_0000078224
Regions
	Topological domain	1 – 59	59	Cytoplasmic Potential
	Transmembrane	60 – 82	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	83 – 775	693	Lumenal Potential
Sites
	Active site	613	1	By similarity
	Metal binding	612	1	Zinc; catalytic By similarity
	Metal binding	616	1	Zinc; catalytic By similarity
	Metal binding	672	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	255	1	N-linked (GlcNAc...) Potential
	Glycosylation	322	1	N-linked (GlcNAc...) Potential
	Glycosylation	656	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	561 – 562	2	Missing in isoform 2.		VSP_017544
	Natural variant	10	1	H → Q. Corresponds to variant rs2741281 [ dbSNP | Ensembl ].		VAR_012813
	Natural variant	328	1	H → Y. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Corresponds to variant rs1529874 [ dbSNP | Ensembl ].		VAR_012814
Experimental info
	Sequence conflict	45	1	A → V in AAQ89282. Ref.4
	Sequence conflict	124	1	Q → R in AAZ22338. Ref.3
	Sequence conflict	152	1	A → T in AAZ22338. Ref.3
	Sequence conflict	163	1	R → C in AAZ22338. Ref.3
	Sequence conflict	286	1	I → V in CAA76113. Ref.1
	Sequence conflict	293	1	F → L in AAZ22338. Ref.3
	Sequence conflict	544	1	R → P in AAQ89282. Ref.4
	Sequence conflict	679	1	G → V in AAQ89282. Ref.4
	Sequence conflict	757 – 758	2	AF → VL in CAA76113. Ref.1
	Sequence conflict	763	1	D → V in CAA76113. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 21, 2006. Version 3. Checksum: C4ED98DE848BE822	FASTA	775	87,791
	10 20 30 40 50 60 MEPPYSLTAH YDEFQEVKYV SRCGAGGARG ASLPPGFPLG AARSATGARS GLPRWNRREV 70 80 90 100 110 120 CLLSGLVFAA GLCAILAAML ALKYLGPVAA GGGACPEGCP ERKAFARAAR FLAANLDASI 130 140 150 160 170 180 DPCQDFYSFA CGGWLRRHAI PDDKLTYGTI AAIGEQNEER LRRLLARPGG GPGGAAQRKV 190 200 210 220 230 240 RAFFRSCLDM REIERLGPRP MLEVIEDCGG WDLGGAEERP GVAARWDLNR LLYKAQGVYS 250 260 270 280 290 300 AAALFSLTVS LDDRNSSRYV IRIDQDGLTL PERTLYLAQD EDSEKILAAY RVFMERVLSL 310 320 330 340 350 360 LGADAVEQKA QEILQVEQQL ANITVSEHDD LRRDVSSMYN KVTLGQLQKI TPHLRWKWLL 370 380 390 400 410 420 DQIFQEDFSE EEEVVLLATD YMQQVSQLIR STPHRVLHNY LVWRVVVVLS EHLSPPFREA 430 440 450 460 470 480 LHELAQEMEG SDKPQELARV CLGQANRHFG MALGALFVHE HFSAASKAKV QQLVEDIKYI 490 500 510 520 530 540 LGQRLEELDW MDAETRAAAR AKLQYMMVMV GYPDFLLKPD AVDKEYEFEV HEKTYFKNIL 550 560 570 580 590 600 NSIRFSIQLS VKKIRQEVDK STWLLPPQAL NAYYLPNKNQ MVFPAGILQP TLYDPDFPQS 610 620 630 640 650 660 LNYGGIGTII GHELTHGYDD WGGQYDRSGN LLHWWTEASY SRFLRKAECI VRLYDNFTVY 670 680 690 700 710 720 NQRVNGKHTL GENIADMGGL KLAYHAYQKW VREHGPEHPL PRLKYTHDQL FFIAFAQNWC 730 740 750 760 770 IKRRSQSIYL QVLTDKHAPE HYRVLGSVSQ FEEFGRAFHC PKDSPMNPAH KCSVW
	Isoform 2 [UniParc]. Checksum: 56AADA3EB8A1A6E0	FASTA	773	87,603
	10 20 30 40 50 60 MEPPYSLTAH YDEFQEVKYV SRCGAGGARG ASLPPGFPLG AARSATGARS GLPRWNRREV 70 80 90 100 110 120 CLLSGLVFAA GLCAILAAML ALKYLGPVAA GGGACPEGCP ERKAFARAAR FLAANLDASI 130 140 150 160 170 180 DPCQDFYSFA CGGWLRRHAI PDDKLTYGTI AAIGEQNEER LRRLLARPGG GPGGAAQRKV 190 200 210 220 230 240 RAFFRSCLDM REIERLGPRP MLEVIEDCGG WDLGGAEERP GVAARWDLNR LLYKAQGVYS 250 260 270 280 290 300 AAALFSLTVS LDDRNSSRYV IRIDQDGLTL PERTLYLAQD EDSEKILAAY RVFMERVLSL 310 320 330 340 350 360 LGADAVEQKA QEILQVEQQL ANITVSEHDD LRRDVSSMYN KVTLGQLQKI TPHLRWKWLL 370 380 390 400 410 420 DQIFQEDFSE EEEVVLLATD YMQQVSQLIR STPHRVLHNY LVWRVVVVLS EHLSPPFREA 430 440 450 460 470 480 LHELAQEMEG SDKPQELARV CLGQANRHFG MALGALFVHE HFSAASKAKV QQLVEDIKYI 490 500 510 520 530 540 LGQRLEELDW MDAETRAAAR AKLQYMMVMV GYPDFLLKPD AVDKEYEFEV HEKTYFKNIL 550 560 570 580 590 600 NSIRFSIQLS VKKIRQEVDK WLLPPQALNA YYLPNKNQMV FPAGILQPTL YDPDFPQSLN 610 620 630 640 650 660 YGGIGTIIGH ELTHGYDDWG GQYDRSGNLL HWWTEASYSR FLRKAECIVR LYDNFTVYNQ 670 680 690 700 710 720 RVNGKHTLGE NIADMGGLKL AYHAYQKWVR EHGPEHPLPR LKYTHDQLFF IAFAQNWCIK 730 740 750 760 770 RRSQSIYLQV LTDKHAPEHY RVLGSVSQFE EFGRAFHCPK DSPMNPAHKC SVW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"XCE, a new member of the endothelin-converting enzyme and neutral endopeptidase family, is preferentially expressed in the CNS." Valdenaire O., Richards J.G., Faull R.L.M., Schweizer A. Brain Res. Mol. Brain Res. 64:211-221(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TYR-328. Tissue: Caudate nucleus and Spinal cord.
[2]	"Organization and chromosomal localization of the human ECEL1 (XCE) gene encoding a zinc metallopeptidase involved in the nervous control of respiration." Valdenaire O., Rohrbacher E., Langeveld A., Schweizer A., Meijers C. Biochem. J. 346:611-616(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-328.
[3]	Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Huang B., Li H., Yang S. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT TYR-328.
[4]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TYR-328.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [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 TYR-328. Tissue: PNS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y16187 mRNA. Translation: CAA76113.1. AJ130734 Genomic DNA. Translation: CAB86601.1. DQ114476 mRNA. Translation: AAZ22338.1. AY358923 mRNA. Translation: AAQ89282.1. AC092165 Genomic DNA. Translation: AAY24101.1. BC050453 mRNA. Translation: AAH50453.2.
IPI	IPI00006735. IPI00741957.
RefSeq	NP_004817.2. NM_004826.2.
UniGene	Hs.26880.
3D structure databases
ProteinModelPortal	O95672.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000302051.
Protein family/group databases
MEROPS	M13.007.
PTM databases
PhosphoSite	O95672.
Proteomic databases
PaxDb	O95672.
PRIDE	O95672.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304546; ENSP00000302051; ENSG00000171551. ENST00000409941; ENSP00000386333; ENSG00000171551.
GeneID	9427.
KEGG	hsa:9427.
UCSC	uc002vsv.2. human. uc010fya.1. human.
Organism-specific databases
CTD	9427.
GeneCards	GC02M233308.
H-InvDB	HIX0029775. HIX0030407.
HGNC	HGNC:3147. ECEL1.
MIM	605896. gene.
neXtProt	NX_O95672.
PharmGKB	PA27595.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3590.
HOGENOM	HOG000245574.
HOVERGEN	HBG005554.
InParanoid	O95672.
KO	K09610.
OMA	SGLPRWN.
OrthoDB	EOG444KJN.
PhylomeDB	O95672.
Gene expression databases
ArrayExpress	O95672.
Bgee	O95672.
CleanEx	HS_ECEL1.
Genevestigator	O95672.
GermOnline	ENSG00000171551. Homo sapiens.
Family and domain databases
Gene3D	3.40.390.10. 2 hits.
InterPro	IPR024079. MetalloPept_cat_dom. IPR000718. Peptidase_M13. IPR018497. Peptidase_M13_C. IPR008753. Peptidase_M13_N. [Graphical view]
PANTHER	PTHR11733. PTHR11733. 1 hit.
Pfam	PF01431. Peptidase_M13. 1 hit. PF05649. Peptidase_M13_N. 1 hit. [Graphical view]
PRINTS	PR00786. NEPRILYSIN.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9427.
NextBio	35318.
SOURCE	Search...

Entry information

Entry name

ECEL1_HUMAN

Accession

Primary (citable) accession number: O95672
Secondary accession number(s): Q45UD9 , Q53RF9, Q6UW86, Q86TH4, Q9NY95

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	March 21, 2006
Last modified:	May 1, 2013
This is version 109 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.