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Protein

Chymotrypsin-like elastase family member 1

Gene

CELA1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts upon elastin.

Catalytic activityi

Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711Charge relay system2 Publications
Metal bindingi85 – 851Calcium
Metal bindingi90 – 901Calcium; via carbonyl oxygen
Metal bindingi95 – 951Calcium
Active sitei119 – 1191Charge relay system1 Publication
Active sitei214 – 2141Charge relay system1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.36. 6170.

Protein family/group databases

MEROPSiS01.153.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsin-like elastase family member 1 (EC:3.4.21.36)
Alternative name(s):
Elastase-1
Gene namesi
Name:CELA1
Synonyms:ELA1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Propeptidei17 – 2610Activation peptide2 PublicationsPRO_0000027681
Chaini27 – 266240Chymotrypsin-like elastase family member 1PRO_0000027682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 72PROSITE-ProRule annotation1 Publication
Disulfide bondi153 ↔ 220
Disulfide bondi184 ↔ 200
Disulfide bondi210 ↔ 240

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP00772.

Expressioni

Tissue specificityi

Pancreas. Basal layers of the epidermis, hair follicle and sebaceous gland epithelia (at protein level).1 Publication

Gene expression databases

GenevisibleiP00772. SS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SERPINA1P010092EBI-986248,EBI-986224From a different organism.

Protein-protein interaction databases

BioGridi1148920. 1 interaction.
DIPiDIP-378N.
IntActiP00772. 1 interaction.
MINTiMINT-1519161.
STRINGi9823.ENSSSCP00000026330.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni35 – 373Combined sources
Beta strandi41 – 488Combined sources
Beta strandi51 – 6212Combined sources
Beta strandi65 – 684Combined sources
Helixi70 – 734Combined sources
Beta strandi74 – 763Combined sources
Beta strandi79 – 846Combined sources
Beta strandi87 – 904Combined sources
Beta strandi96 – 10510Combined sources
Beta strandi111 – 1133Combined sources
Helixi114 – 1163Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi153 – 1586Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi172 – 1754Combined sources
Helixi181 – 1844Combined sources
Turni187 – 1904Combined sources
Helixi191 – 1933Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi204 – 2063Combined sources
Turni211 – 2155Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi225 – 23410Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi247 – 2515Combined sources
Helixi252 – 2543Combined sources
Helixi256 – 26510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0EX-ray1.80A27-266[»]
1BMAX-ray1.80A27-266[»]
1BTUX-ray1.60A27-266[»]
1C1MX-ray2.20A27-266[»]
1E34X-ray1.80B27-266[»]
1E35X-ray1.90B27-266[»]
1E36X-ray1.70B27-266[»]
1E37X-ray1.75B27-266[»]
1E38X-ray1.70B27-266[»]
1EAIX-ray2.40A/B27-266[»]
1EASX-ray1.80A27-266[»]
1EATX-ray2.00A27-266[»]
1EAUX-ray2.00A27-266[»]
1ELAX-ray2.00A27-266[»]
1ELBX-ray2.10A27-266[»]
1ELCX-ray1.75A27-266[»]
1ELDX-ray2.00E27-266[»]
1ELEX-ray2.00E27-266[»]
1ELFX-ray1.70A27-266[»]
1ELGX-ray1.65A27-266[»]
1ESAX-ray1.65A27-266[»]
1ESBX-ray2.30A27-266[»]
1ESTX-ray2.50A27-266[»]
1FLEX-ray1.90E27-266[»]
1FZZX-ray1.86A27-266[»]
1GVKX-ray0.94B27-266[»]
1GWAX-ray1.85A27-266[»]
1H9LX-ray1.67B27-266[»]
1HAXX-ray1.60B27-266[»]
1HAYX-ray1.70B27-266[»]
1HAZX-ray1.40B27-266[»]
1HB0X-ray2.05B27-266[»]
1HV7X-ray1.70A27-266[»]
1INCX-ray1.94A27-266[»]
1JIMX-ray2.31A27-266[»]
1L0ZX-ray1.50A27-266[»]
1L1GX-ray1.50A27-266[»]
1LKAX-ray1.70A27-266[»]
1LKBX-ray1.70A27-266[»]
1LVYX-ray1.87A27-266[»]
1MCVX-ray1.80A27-266[»]
1MMJX-ray2.20N27-266[»]
1NESX-ray1.65E27-266[»]
1OKXX-ray2.80A/B27-266[»]
1QGFX-ray1.70A27-266[»]
1QIXX-ray1.90B27-266[»]
1QNJX-ray1.10A27-266[»]
1QR3X-ray1.60E27-266[»]
1UO6X-ray1.65A27-266[»]
1UVOX-ray1.85A27-266[»]
1UVPX-ray1.85A27-266[»]
2A7CX-ray1.65A27-266[»]
2A7JX-ray1.65A27-266[»]
2BB4X-ray1.60A27-266[»]
2BD2X-ray1.70A27-266[»]
2BD3X-ray1.60A27-266[»]
2BD4X-ray1.70A27-266[»]
2BD5X-ray1.80A27-266[»]
2BD7X-ray1.60A27-266[»]
2BD8X-ray1.70A27-266[»]
2BD9X-ray1.90A27-266[»]
2BDAX-ray1.80A27-266[»]
2BDBX-ray1.70A27-266[»]
2BDCX-ray1.80A27-266[»]
2BLOX-ray1.33A27-266[»]
2BLQX-ray1.33A27-266[»]
2CV3X-ray1.90A27-266[»]
2D26X-ray3.30C27-266[»]
2DE8X-ray1.50A27-266[»]
2DE9X-ray1.30A27-266[»]
2ESTX-ray2.50E27-266[»]
2FO9X-ray2.00A27-266[»]
2FOAX-ray1.90A27-266[»]
2FOBX-ray1.90A27-266[»]
2FOCX-ray2.00A27-266[»]
2FODX-ray2.00A27-266[»]
2FOEX-ray2.20A27-266[»]
2FOFX-ray2.20A27-266[»]
2FOGX-ray1.90A27-266[»]
2FOHX-ray1.80A27-266[»]
2G4TX-ray2.15A27-266[»]
2G4UX-ray1.84A27-266[»]
2H1UX-ray1.60A27-266[»]
2IOTX-ray1.60A27-266[»]
2OQUX-ray1.80A27-266[»]
2V0BX-ray1.65A27-266[»]
2V35X-ray1.67A27-266[»]
3E3TX-ray1.60A27-266[»]
3ESTX-ray1.65A27-266[»]
3HGNOther1.65A27-266[»]
3HGPX-ray0.94A27-266[»]
3MNBX-ray1.20A27-266[»]
3MNCX-ray1.12A27-266[»]
3MNSX-ray1.50A27-266[»]
3MNXX-ray1.39A27-266[»]
3MO3X-ray1.80A27-266[»]
3MO6X-ray1.66A27-266[»]
3MO9X-ray2.00A27-266[»]
3MOCX-ray1.82A27-266[»]
3MTYX-ray1.10A27-266[»]
3MU0X-ray1.40A27-266[»]
3MU1X-ray1.74A27-266[»]
3MU4X-ray1.10A27-266[»]
3MU5X-ray1.40A27-266[»]
3MU8X-ray1.55A27-266[»]
3ODDX-ray1.10A27-266[»]
3ODFX-ray1.10A27-266[»]
3UOUX-ray2.00A27-266[»]
4ESTX-ray1.78E27-266[»]
4GVUX-ray1.55A27-266[»]
5ESTX-ray2.09E27-266[»]
6ESTX-ray1.80A27-266[»]
7ESTX-ray1.80E27-266[»]
8ESTX-ray1.78E27-266[»]
9ESTX-ray1.90A27-266[»]
ProteinModelPortaliP00772.
SMRiP00772. Positions 27-266.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00772.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 264238Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
InParanoidiP00772.
KOiK01326.
OMAiAHCVDYQ.
OrthoDBiEOG7RRF7Z.
TreeFamiTF330455.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. 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.

P00772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLLVVASL VLYGHSTQDF PETNARVVGG TEAQRNSWPS QISLQYRSGS
60 70 80 90 100
SWAHTCGGTL IRQNWVMTAA HCVDRELTFR VVVGEHNLNQ NDGTEQYVGV
110 120 130 140 150
QKIVVHPYWN TDDVAAGYDI ALLRLAQSVT LNSYVQLGVL PRAGTILANN
160 170 180 190 200
SPCYITGWGL TRTNGQLAQT LQQAYLPTVD YAICSSSSYW GSTVKNSMVC
210 220 230 240 250
AGGDGVRSGC QGDSGGPLHC LVNGQYAVHG VTSFVSRLGC NVTRKPTVFT
260
RVSAYISWIN NVIASN
Length:266
Mass (Da):28,821
Last modified:April 1, 1988 - v1
Checksum:iBF07D6855BB50FE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921D → N AA sequence (PubMed:4578945).Curated
Sequence conflicti126 – 1261A → G in BAA00118 (PubMed:3648024).Curated
Sequence conflicti184 – 1841C → L in BAA00118 (PubMed:3648024).Curated
Sequence conflicti204 – 2041D → N AA sequence (PubMed:4578945).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04036 Transcribed RNA. Translation: CAA27670.1.
D00160 mRNA. Translation: BAA00118.1.
PIRiJS0013. ELPG.
RefSeqiNP_998988.1. NM_213823.1.
XP_005655631.1. XM_005655574.1.
UniGeneiSsc.5575.
Ssc.89635.

Genome annotation databases

EnsembliENSSSCT00000030908; ENSSSCP00000026330; ENSSSCG00000029782.
GeneIDi396766.
KEGGissc:396766.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04036 Transcribed RNA. Translation: CAA27670.1.
D00160 mRNA. Translation: BAA00118.1.
PIRiJS0013. ELPG.
RefSeqiNP_998988.1. NM_213823.1.
XP_005655631.1. XM_005655574.1.
UniGeneiSsc.5575.
Ssc.89635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0EX-ray1.80A27-266[»]
1BMAX-ray1.80A27-266[»]
1BTUX-ray1.60A27-266[»]
1C1MX-ray2.20A27-266[»]
1E34X-ray1.80B27-266[»]
1E35X-ray1.90B27-266[»]
1E36X-ray1.70B27-266[»]
1E37X-ray1.75B27-266[»]
1E38X-ray1.70B27-266[»]
1EAIX-ray2.40A/B27-266[»]
1EASX-ray1.80A27-266[»]
1EATX-ray2.00A27-266[»]
1EAUX-ray2.00A27-266[»]
1ELAX-ray2.00A27-266[»]
1ELBX-ray2.10A27-266[»]
1ELCX-ray1.75A27-266[»]
1ELDX-ray2.00E27-266[»]
1ELEX-ray2.00E27-266[»]
1ELFX-ray1.70A27-266[»]
1ELGX-ray1.65A27-266[»]
1ESAX-ray1.65A27-266[»]
1ESBX-ray2.30A27-266[»]
1ESTX-ray2.50A27-266[»]
1FLEX-ray1.90E27-266[»]
1FZZX-ray1.86A27-266[»]
1GVKX-ray0.94B27-266[»]
1GWAX-ray1.85A27-266[»]
1H9LX-ray1.67B27-266[»]
1HAXX-ray1.60B27-266[»]
1HAYX-ray1.70B27-266[»]
1HAZX-ray1.40B27-266[»]
1HB0X-ray2.05B27-266[»]
1HV7X-ray1.70A27-266[»]
1INCX-ray1.94A27-266[»]
1JIMX-ray2.31A27-266[»]
1L0ZX-ray1.50A27-266[»]
1L1GX-ray1.50A27-266[»]
1LKAX-ray1.70A27-266[»]
1LKBX-ray1.70A27-266[»]
1LVYX-ray1.87A27-266[»]
1MCVX-ray1.80A27-266[»]
1MMJX-ray2.20N27-266[»]
1NESX-ray1.65E27-266[»]
1OKXX-ray2.80A/B27-266[»]
1QGFX-ray1.70A27-266[»]
1QIXX-ray1.90B27-266[»]
1QNJX-ray1.10A27-266[»]
1QR3X-ray1.60E27-266[»]
1UO6X-ray1.65A27-266[»]
1UVOX-ray1.85A27-266[»]
1UVPX-ray1.85A27-266[»]
2A7CX-ray1.65A27-266[»]
2A7JX-ray1.65A27-266[»]
2BB4X-ray1.60A27-266[»]
2BD2X-ray1.70A27-266[»]
2BD3X-ray1.60A27-266[»]
2BD4X-ray1.70A27-266[»]
2BD5X-ray1.80A27-266[»]
2BD7X-ray1.60A27-266[»]
2BD8X-ray1.70A27-266[»]
2BD9X-ray1.90A27-266[»]
2BDAX-ray1.80A27-266[»]
2BDBX-ray1.70A27-266[»]
2BDCX-ray1.80A27-266[»]
2BLOX-ray1.33A27-266[»]
2BLQX-ray1.33A27-266[»]
2CV3X-ray1.90A27-266[»]
2D26X-ray3.30C27-266[»]
2DE8X-ray1.50A27-266[»]
2DE9X-ray1.30A27-266[»]
2ESTX-ray2.50E27-266[»]
2FO9X-ray2.00A27-266[»]
2FOAX-ray1.90A27-266[»]
2FOBX-ray1.90A27-266[»]
2FOCX-ray2.00A27-266[»]
2FODX-ray2.00A27-266[»]
2FOEX-ray2.20A27-266[»]
2FOFX-ray2.20A27-266[»]
2FOGX-ray1.90A27-266[»]
2FOHX-ray1.80A27-266[»]
2G4TX-ray2.15A27-266[»]
2G4UX-ray1.84A27-266[»]
2H1UX-ray1.60A27-266[»]
2IOTX-ray1.60A27-266[»]
2OQUX-ray1.80A27-266[»]
2V0BX-ray1.65A27-266[»]
2V35X-ray1.67A27-266[»]
3E3TX-ray1.60A27-266[»]
3ESTX-ray1.65A27-266[»]
3HGNOther1.65A27-266[»]
3HGPX-ray0.94A27-266[»]
3MNBX-ray1.20A27-266[»]
3MNCX-ray1.12A27-266[»]
3MNSX-ray1.50A27-266[»]
3MNXX-ray1.39A27-266[»]
3MO3X-ray1.80A27-266[»]
3MO6X-ray1.66A27-266[»]
3MO9X-ray2.00A27-266[»]
3MOCX-ray1.82A27-266[»]
3MTYX-ray1.10A27-266[»]
3MU0X-ray1.40A27-266[»]
3MU1X-ray1.74A27-266[»]
3MU4X-ray1.10A27-266[»]
3MU5X-ray1.40A27-266[»]
3MU8X-ray1.55A27-266[»]
3ODDX-ray1.10A27-266[»]
3ODFX-ray1.10A27-266[»]
3UOUX-ray2.00A27-266[»]
4ESTX-ray1.78E27-266[»]
4GVUX-ray1.55A27-266[»]
5ESTX-ray2.09E27-266[»]
6ESTX-ray1.80A27-266[»]
7ESTX-ray1.80E27-266[»]
8ESTX-ray1.78E27-266[»]
9ESTX-ray1.90A27-266[»]
ProteinModelPortaliP00772.
SMRiP00772. Positions 27-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1148920. 1 interaction.
DIPiDIP-378N.
IntActiP00772. 1 interaction.
MINTiMINT-1519161.
STRINGi9823.ENSSSCP00000026330.

Chemistry

BindingDBiP00772.
ChEMBLiCHEMBL3517.

Protein family/group databases

MEROPSiS01.153.

Proteomic databases

PRIDEiP00772.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000030908; ENSSSCP00000026330; ENSSSCG00000029782.
GeneIDi396766.
KEGGissc:396766.

Organism-specific databases

CTDi1990.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119027.
InParanoidiP00772.
KOiK01326.
OMAiAHCVDYQ.
OrthoDBiEOG7RRF7Z.
TreeFamiTF330455.

Enzyme and pathway databases

BRENDAi3.4.21.36. 6170.

Miscellaneous databases

EvolutionaryTraceiP00772.
PROiP00772.

Gene expression databases

GenevisibleiP00772. SS.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and expression in Escherichia coli of a cDNA clone encoding porcine pancreatic elastase."
    Shirasu Y., Yoshida H., Mikayama T., Matsuki S., Tanaka J., Ikenaga H.
    J. Biochem. 99:1707-1712(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Characterization of a silent gene for human pancreatic elastase I: structure of the 5'-flanking region."
    Tani T., Kawashima I., Furukawa H., Ohmine T., Takiguchi Y.
    J. Biochem. 101:591-599(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Evidence for the amino acid sequence of porcine pancreatic elastase."
    Shotton D.M., Hartley B.S.
    Biochem. J. 131:643-675(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-266.
  4. "Amino-acid sequence of porcine pancreatic elastase and its homologies with other serine proteinases."
    Shotton D.M., Hartley B.S.
    Nature 225:802-806(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-266.
  5. "Human elastase 1: evidence for expression in the skin and the identification of a frequent frameshift polymorphism."
    Talas U., Dunlop J., Khalaf S., Leigh I.M., Kelsell D.P.
    J. Invest. Dermatol. 114:165-170(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "The atomic structure of crystalline porcine pancreatic elastase at 2.5-A resolution: comparisons with the structure of alpha-chymotrypsin."
    Sawyer L., Shotton D.M., Campbell J.W., Wendell P.L., Muirhead H., Watson H.C., Diamond R., Ladner R.C.
    J. Mol. Biol. 118:137-208(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  7. "Three-dimensional structure of tosyl-elastase."
    Shotton D.M., Watson H.C.
    Nature 225:811-816(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), ACTIVE SITE.
  8. "The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase."
    Huang K., Strynadka N.C., Bernard V.D., Peanasky R.J., James M.N.
    Structure 2:679-689(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH INHIBITOR.

Entry informationi

Entry nameiCELA1_PIG
AccessioniPrimary (citable) accession number: P00772
Secondary accession number(s): Q29625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: June 24, 2015
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.