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Protein

Enteropeptidase

Gene

TMPRSS15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.

Catalytic activityi

Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei825 – 8251Charge relay systemBy similarity
Active sitei876 – 8761Charge relay systemBy similarity
Active sitei971 – 9711Charge relay systemBy similarity

GO - Molecular functioni

  1. scavenger receptor activity Source: InterPro
  2. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.9. 2681.

Protein family/group databases

MEROPSiS01.156.

Names & Taxonomyi

Protein namesi
Recommended name:
Enteropeptidase (EC:3.4.21.9)
Alternative name(s):
Enterokinase
Serine protease 7
Transmembrane protease serine 15
Cleaved into the following 2 chains:
Gene namesi
Name:TMPRSS15
Synonyms:ENTK, PRSS7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:9490. TMPRSS15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1817CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei19 – 4729Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini48 – 1019972ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. brush border Source: ProtInc
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Enterokinase deficiency1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionLife-threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive.

See also OMIM:226200

Organism-specific databases

MIMi226200. phenotype.
Orphaneti168601. Congenital enteropathy due to enteropeptidase deficiency.
PharmGKBiPA33839.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedSequence Analysis
Chaini2 – 784783Enteropeptidase non-catalytic heavy chainPRO_0000027719Add
BLAST
Chaini785 – 1019235Enteropeptidase catalytic light chainPRO_0000027720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi184 ↔ 197By similarity
Disulfide bondi191 ↔ 210By similarity
Disulfide bondi204 ↔ 221By similarity
Disulfide bondi225 ↔ 253By similarity
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi503 – 5031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi524 ↔ 552By similarity
Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi630 – 6301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi643 ↔ 655By similarity
Disulfide bondi650 ↔ 668By similarity
Disulfide bondi662 ↔ 677By similarity
Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi706 – 7061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi725 – 7251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi757 ↔ 767By similarity
Disulfide bondi772 ↔ 896Interchain (between heavy and light chains)PROSITE-ProRule annotation
Disulfide bondi810 ↔ 8261 Publication
Glycosylationi848 – 8481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi887 – 8871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi909 – 9091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi910 ↔ 9771 Publication
Disulfide bondi941 ↔ 9561 Publication
Glycosylationi949 – 9491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi967 ↔ 9951 Publication

Post-translational modificationi

The chains are derived from a single precursor that is cleaved by a trypsin-like protease.

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate, Zymogen

Proteomic databases

PaxDbiP98073.
PRIDEiP98073.

PTM databases

PhosphoSiteiP98073.

Expressioni

Tissue specificityi

Intestinal brush border.

Gene expression databases

BgeeiP98073.
CleanExiHS_PRSS7.
ExpressionAtlasiP98073. baseline and differential.
GenevestigatoriP98073.

Organism-specific databases

HPAiHPA015611.

Interactioni

Subunit structurei

Heterodimer of a catalytic (light) chain and a multidomain (heavy) chain linked by a disulfide bond.

Protein-protein interaction databases

IntActiP98073. 2 interactions.

Structurei

Secondary structure

1
1019
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi799 – 8046Combined sources
Beta strandi807 – 8148Combined sources
Beta strandi816 – 8227Combined sources
Helixi824 – 8274Combined sources
Helixi834 – 8363Combined sources
Beta strandi837 – 8426Combined sources
Beta strandi855 – 86410Combined sources
Turni870 – 8734Combined sources
Beta strandi878 – 8847Combined sources
Beta strandi909 – 91911Combined sources
Beta strandi929 – 9368Combined sources
Helixi938 – 9447Combined sources
Beta strandi954 – 9574Combined sources
Beta strandi974 – 9796Combined sources
Beta strandi982 – 99110Combined sources
Beta strandi993 – 9964Combined sources
Beta strandi1002 – 10065Combined sources
Helixi1007 – 10093Combined sources
Helixi1011 – 10155Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DGJX-ray1.90A/B/C/D785-1019[»]
ProteinModelPortaliP98073.
SMRiP98073. Positions 271-510, 523-658, 748-1019.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 169116SEAPROSITE-ProRule annotationAdd
BLAST
Domaini182 – 22342LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini225 – 334110CUB 1PROSITE-ProRule annotationAdd
BLAST
Domaini342 – 504163MAMPROSITE-ProRule annotationAdd
BLAST
Domaini524 – 634111CUB 2PROSITE-ProRule annotationAdd
BLAST
Domaini641 – 67939LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini678 – 77194SRCRPROSITE-ProRule annotationAdd
BLAST
Domaini785 – 1019235Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 2 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 1 MAM domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 1 SEA domain.PROSITE-ProRule annotation
Contains 1 SRCR domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000112380.
HOVERGENiHBG005588.
InParanoidiP98073.
KOiK01316.
OMAiFEDGFCF.
OrthoDBiEOG7RNK07.
PhylomeDBiP98073.
TreeFamiTF351678.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
3.10.250.10. 1 hit.
3.30.70.960. 1 hit.
4.10.400.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR000998. MAM_dom.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00057. Ldl_recept_a. 1 hit.
PF00629. MAM. 1 hit.
PF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00042. CUB. 2 hits.
SM00192. LDLa. 2 hits.
SM00137. MAM. 1 hit.
SM00200. SEA. 1 hit.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 2 hits.
SSF82671. SSF82671. 1 hit.
PROSITEiPS01180. CUB. 2 hits.
PS01209. LDLRA_1. 2 hits.
PS50068. LDLRA_2. 2 hits.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
PS50024. SEA. 1 hit.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P98073-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSKRGISSR HHSLSSYEIM FAALFAILVV LCAGLIAVSC LTIKESQRGA
60 70 80 90 100
ALGQSHEARA TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS
110 120 130 140 150
NLKNEYKNSR VLQFENGSII VVFDLFFAQW VSDENVKEEL IQGLEANKSS
160 170 180 190 200
QLVTFHIDLN SVDILDKLTT TSHLATPGNV SIECLPGSSP CTDALTCIKA
210 220 230 240 250
DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA THYPKPSETS
260 270 280 290 300
VVCQWIIRVN QGLSIKLSFD DFNTYYTDIL DIYEGVGSSK ILRASIWETN
310 320 330 340 350
PGTIRIFSNQ VTATFLIESD ESDYVGFNAT YTAFNSSELN NYEKINCNFE
360 370 380 390 400
DGFCFWVQDL NDDNEWERIQ GSTFSPFTGP NFDHTFGNAS GFYISTPTGP
410 420 430 440 450
GGRQERVGLL SLPLDPTLEP ACLSFWYHMY GENVHKLSIN ISNDQNMEKT
460 470 480 490 500
VFQKEGNYGD NWNYGQVTLN ETVKFKVAFN AFKNKILSDI ALDDISLTYG
510 520 530 540 550
ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSST NFPNSYPNLA
560 570 580 590 600
FCVWILNAQK GKNIQLHFQE FDLENINDVV EIRDGEEADS LLLAVYTGPG
610 620 630 640 650
PVKDVFSTTN RMTVLLITND VLARGGFKAN FTTGYHLGIP EPCKADHFQC
660 670 680 690 700
KNGECVPLVN LCDGHLHCED GSDEADCVRF FNGTTNNNGL VRFRIQSIWH
710 720 730 740 750
TACAENWTTQ ISNDVCQLLG LGSGNSSKPI FPTDGGPFVK LNTAPDGHLI
760 770 780 790 800
LTPSQQCLQD SLIRLQCNHK SCGKKLAAQD ITPKIVGGSN AKEGAWPWVV
810 820 830 840 850
GLYYGGRLLC GASLVSSDWL VSAAHCVYGR NLEPSKWTAI LGLHMKSNLT
860 870 880 890 900
SPQTVPRLID EIVINPHYNR RRKDNDIAMM HLEFKVNYTD YIQPICLPEE
910 920 930 940 950
NQVFPPGRNC SIAGWGTVVY QGTTANILQE ADVPLLSNER CQQQMPEYNI
960 970 980 990 1000
TENMICAGYE EGGIDSCQGD SGGPLMCQEN NRWFLAGVTS FGYKCALPNR
1010
PGVYARVSRF TEWIQSFLH
Length:1,019
Mass (Da):112,935
Last modified:January 11, 2011 - v3
Checksum:i45288F0636E5EC52
GO

Sequence cautioni

The sequence CAB90389.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651T → I.
Corresponds to variant rs35987974 [ dbSNP | Ensembl ].
VAR_031686
Natural varianti77 – 771K → R.
Corresponds to variant rs2824804 [ dbSNP | Ensembl ].
VAR_021940
Natural varianti134 – 1341E → Q.3 Publications
Corresponds to variant rs2824790 [ dbSNP | Ensembl ].
VAR_031687
Natural varianti545 – 5451S → C.
Corresponds to variant rs8134187 [ dbSNP | Ensembl ].
VAR_031688
Natural varianti641 – 6411E → K.
Corresponds to variant rs2273204 [ dbSNP | Ensembl ].
VAR_020175
Natural varianti660 – 6601N → H.
Corresponds to variant rs11088674 [ dbSNP | Ensembl ].
VAR_024292
Natural varianti732 – 7321P → S.3 Publications
Corresponds to variant rs2824721 [ dbSNP | Ensembl ].
VAR_031689
Natural varianti828 – 8281Y → C.
Corresponds to variant rs8130110 [ dbSNP | Ensembl ].
VAR_031690

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09860 mRNA. Translation: AAC50138.1.
Y19124
, Y19125, Y19126, Y19127, Y19128, Y19129, Y19130, Y19131, Y19132, Y19133, Y19134, Y19135, Y19136, Y19137, Y19138, Y19139, Y19140, Y19141, Y19142, Y19143 Genomic DNA. Translation: CAB65555.1.
AL163217 Genomic DNA. Translation: CAB90389.1. Sequence problems.
AL163218 Genomic DNA. Translation: CAB90392.1.
BC111749 mRNA. Translation: AAI11750.1.
CCDSiCCDS13571.1.
PIRiA56318.
RefSeqiNP_002763.2. NM_002772.2.
UniGeneiHs.149473.

Genome annotation databases

EnsembliENST00000284885; ENSP00000284885; ENSG00000154646.
GeneIDi5651.
KEGGihsa:5651.
UCSCiuc002ykw.3. human.

Polymorphism databases

DMDMi317373442.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09860 mRNA. Translation: AAC50138.1.
Y19124
, Y19125, Y19126, Y19127, Y19128, Y19129, Y19130, Y19131, Y19132, Y19133, Y19134, Y19135, Y19136, Y19137, Y19138, Y19139, Y19140, Y19141, Y19142, Y19143 Genomic DNA. Translation: CAB65555.1.
AL163217 Genomic DNA. Translation: CAB90389.1. Sequence problems.
AL163218 Genomic DNA. Translation: CAB90392.1.
BC111749 mRNA. Translation: AAI11750.1.
CCDSiCCDS13571.1.
PIRiA56318.
RefSeqiNP_002763.2. NM_002772.2.
UniGeneiHs.149473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DGJX-ray1.90A/B/C/D785-1019[»]
ProteinModelPortaliP98073.
SMRiP98073. Positions 271-510, 523-658, 748-1019.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP98073. 2 interactions.

Chemistry

BindingDBiP98073.
ChEMBLiCHEMBL1741195.

Protein family/group databases

MEROPSiS01.156.

PTM databases

PhosphoSiteiP98073.

Polymorphism databases

DMDMi317373442.

Proteomic databases

PaxDbiP98073.
PRIDEiP98073.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284885; ENSP00000284885; ENSG00000154646.
GeneIDi5651.
KEGGihsa:5651.
UCSCiuc002ykw.3. human.

Organism-specific databases

CTDi5651.
GeneCardsiGC21M019641.
HGNCiHGNC:9490. TMPRSS15.
HPAiHPA015611.
MIMi226200. phenotype.
606635. gene.
neXtProtiNX_P98073.
Orphaneti168601. Congenital enteropathy due to enteropeptidase deficiency.
PharmGKBiPA33839.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118962.
HOGENOMiHOG000112380.
HOVERGENiHBG005588.
InParanoidiP98073.
KOiK01316.
OMAiFEDGFCF.
OrthoDBiEOG7RNK07.
PhylomeDBiP98073.
TreeFamiTF351678.

Enzyme and pathway databases

BRENDAi3.4.21.9. 2681.

Miscellaneous databases

GenomeRNAii5651.
NextBioi21958.
PROiP98073.
SOURCEiSearch...

Gene expression databases

BgeeiP98073.
CleanExiHS_PRSS7.
ExpressionAtlasiP98073. baseline and differential.
GenevestigatoriP98073.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
3.10.250.10. 1 hit.
3.30.70.960. 1 hit.
4.10.400.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000859. CUB_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR000998. MAM_dom.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000082. SEA_dom.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00057. Ldl_recept_a. 1 hit.
PF00629. MAM. 1 hit.
PF01390. SEA. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00042. CUB. 2 hits.
SM00192. LDLa. 2 hits.
SM00137. MAM. 1 hit.
SM00200. SEA. 1 hit.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 2 hits.
SSF82671. SSF82671. 1 hit.
PROSITEiPS01180. CUB. 2 hits.
PS01209. LDLRA_1. 2 hits.
PS50068. LDLRA_2. 2 hits.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
PS50024. SEA. 1 hit.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence and chromosomal localization of human enterokinase, the proteolytic activator of trypsinogen."
    Kitamoto Y., Veile R.A., Donis-Keller H., Sadler J.E.
    Biochemistry 34:4562-4568(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLN-134 AND SER-732.
    Tissue: Duodenum.
  2. "Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency."
    Holzinger A., Maier E.M., Buck C., Mayerhofer P.U., Kappler M., Haworth J.C., Moroz S.P., Hadorn H.-B., Sadler J.E., Roscher A.A.
    Am. J. Hum. Genet. 70:20-25(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-134 AND SER-732, INVOLVEMENT IN ENTKD.
  3. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS GLN-134 AND SER-732.
  5. "Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains."
    Kitamoto Y., Yuan X., Wu Q., McCourt D.W., Sadler J.E.
    Proc. Natl. Acad. Sci. U.S.A. 91:7588-7592(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 749-1019.
    Tissue: Duodenum.
  6. "Crystal structure of a supercharged variant of the human enteropeptidase light chain."
    Simeonov P., Zahn M., Strater N., Zuchner T.
    Proteins 80:1907-1910(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 785-1019, DISULFIDE BONDS.

Entry informationi

Entry nameiENTK_HUMAN
AccessioniPrimary (citable) accession number: P98073
Secondary accession number(s): Q2NKL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 11, 2011
Last modified: January 7, 2015
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.