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Protein

Salivary plasminogen activator alpha 1

Gene
N/A
Organism
Desmodus rotundus (Vampire bat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably essential to support the feeding habits of this exclusively haematophagous animal. Potent thrombolytic agent.

Catalytic activityi

Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.

Enzyme regulationi

Activity toward plasminogen is stimulated in the presence of fibrin I.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei272 – 2721Charge relay system
Active sitei321 – 3211Charge relay system
Active sitei428 – 4281Charge relay system

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Plasminogen activation

Protein family/group databases

MEROPSiS01.239.

Names & Taxonomyi

Protein namesi
Recommended name:
Salivary plasminogen activator alpha 1 (EC:3.4.21.68)
Alternative name(s):
DSPA alpha-1
OrganismiDesmodus rotundus (Vampire bat)
Taxonomic identifieri9430 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaChiropteraMicrochiropteraPhyllostomidaeDesmodontinaeDesmodus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Sequence analysisAdd
BLAST
Chaini37 – 477441Salivary plasminogen activator alpha 1PRO_0000028340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 72By similarity
Disulfide bondi70 ↔ 79By similarity
Disulfide bondi87 ↔ 98By similarity
Disulfide bondi92 ↔ 109By similarity
Disulfide bondi111 ↔ 120By similarity
Disulfide bondi128 ↔ 209By similarity
Disulfide bondi149 ↔ 191By similarity
Glycosylationi153 – 1531N-linked (GlcNAc...)CAR_000027
Disulfide bondi180 ↔ 204By similarity
Disulfide bondi214 ↔ 345
Disulfide bondi257 ↔ 273
Disulfide bondi265 ↔ 334
Disulfide bondi359 ↔ 434
Disulfide bondi391 ↔ 407
Glycosylationi398 – 3981N-linked (GlcNAc...)CAR_000028
Disulfide bondi424 ↔ 452

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP98119.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi234 – 2363Combined sources
Beta strandi240 – 2456Combined sources
Beta strandi248 – 2514Combined sources
Beta strandi254 – 26310Combined sources
Beta strandi266 – 2694Combined sources
Helixi271 – 2733Combined sources
Turni280 – 2823Combined sources
Beta strandi284 – 2885Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi300 – 30910Combined sources
Turni315 – 3173Combined sources
Beta strandi323 – 3286Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi358 – 3647Combined sources
Beta strandi366 – 3705Combined sources
Beta strandi379 – 3857Combined sources
Helixi388 – 3903Combined sources
Turni393 – 3986Combined sources
Beta strandi405 – 4095Combined sources
Beta strandi414 – 4163Combined sources
Beta strandi431 – 4366Combined sources
Beta strandi439 – 44810Combined sources
Beta strandi450 – 4534Combined sources
Beta strandi459 – 4635Combined sources
Helixi464 – 4674Combined sources
Helixi468 – 4747Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5IX-ray2.90A213-477[»]
ProteinModelPortaliP98119.
SMRiP98119. Positions 37-127, 213-477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98119.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 8243Fibronectin type-IPROSITE-ProRule annotationAdd
BLAST
Domaini83 – 12139EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini128 – 20982KringlePROSITE-ProRule annotationAdd
BLAST
Domaini226 – 476251Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Domaini

The fibronectin type-I domain mediates binding to fibrin, and the kringle domain apparently mediates fibrin-induced stimulation of activity.

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-I domain.PROSITE-ProRule annotation
Contains 1 kringle domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Signal

Phylogenomic databases

HOVERGENiHBG008633.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000083. Fibronectin_type1.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00039. fn1. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00058. FN1. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01253. FN1_1. 1 hit.
PS51091. FN1_2. 1 hit.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_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.

P98119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNTMKTKLL CVLLLCGAVF SLPRQETYRQ LARGSRAYGV ACKDEITQMT
60 70 80 90 100
YRRQESWLRP EVRSKRVEHC QCDRGQARCH TVPVNSCSEP RCFNGGTCWQ
110 120 130 140 150
AVYFSDFVCQ CPAGYTGKRC EVDTRATCYE GQGVTYRGTW STAESRVECI
160 170 180 190 200
NWNSSLLTRR TYNGRMPDAF NLGLGNHNYC RNPNGAPKPW CYVIKAGKFT
210 220 230 240 250
SESCSVPVCS KATCGLRKYK EPQLHSTGGL FTDITSHPWQ AAIFAQNRRS
260 270 280 290 300
SGERFLCGGI LISSCWVLTA AHCFQESYLP DQLKVVLGRT YRVKPGEEEQ
310 320 330 340 350
TFKVKKYIVH KEFDDDTYNN DIALLQLKSD SPQCAQESDS VRAICLPEAN
360 370 380 390 400
LQLPDWTECE LSGYGKHKSS SPFYSEQLKE GHVRLYPSSR CAPKFLFNKT
410 420 430 440 450
VTNNMLCAGD TRSGEIYPNV HDACQGDSGG PLVCMNDNHM TLLGIISWGV
460 470
GCGEKDVPGV YTKVTNYLGW IRDNMHL
Length:477
Mass (Da):53,616
Last modified:February 1, 1996 - v1
Checksum:iAA06FD1739C10E5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63987 mRNA. Translation: AAA31591.1.
M63986 mRNA. Translation: AAA31592.1.
PIRiJS0597.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63987 mRNA. Translation: AAA31591.1.
M63986 mRNA. Translation: AAA31592.1.
PIRiJS0597.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5IX-ray2.90A213-477[»]
ProteinModelPortaliP98119.
SMRiP98119. Positions 37-127, 213-477.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.239.

PTM databases

UniCarbKBiP98119.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008633.

Miscellaneous databases

EvolutionaryTraceiP98119.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000083. Fibronectin_type1.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00039. fn1. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00058. FN1. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01253. FN1_1. 1 hit.
PS51091. FN1_2. 1 hit.
PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiURT1_DESRO
AccessioniPrimary (citable) accession number: P98119
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 7, 2016
This is version 111 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

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

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 one 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.