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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)DescriptionActionsGraphical viewLength
Active sitei272Charge relay system1
Active sitei321Charge relay system1
Active sitei428Charge relay system1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
ChainiPRO_000002834037 – 477Salivary plasminogen activator alpha 1Add BLAST441

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
GlycosylationiCAR_000027153N-linked (GlcNAc...)1
Disulfide bondi180 ↔ 204By similarity
Disulfide bondi214 ↔ 345
Disulfide bondi257 ↔ 273
Disulfide bondi265 ↔ 334
Disulfide bondi359 ↔ 434
Disulfide bondi391 ↔ 407
GlycosylationiCAR_000028398N-linked (GlcNAc...)1
Disulfide bondi424 ↔ 452

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP98119.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi234 – 236Combined sources3
Beta strandi240 – 245Combined sources6
Beta strandi248 – 251Combined sources4
Beta strandi254 – 263Combined sources10
Beta strandi266 – 269Combined sources4
Helixi271 – 273Combined sources3
Turni280 – 282Combined sources3
Beta strandi284 – 288Combined sources5
Beta strandi290 – 294Combined sources5
Beta strandi300 – 309Combined sources10
Turni315 – 317Combined sources3
Beta strandi323 – 328Combined sources6
Beta strandi330 – 332Combined sources3
Beta strandi358 – 364Combined sources7
Beta strandi366 – 370Combined sources5
Beta strandi379 – 385Combined sources7
Helixi388 – 390Combined sources3
Turni393 – 398Combined sources6
Beta strandi405 – 409Combined sources5
Beta strandi414 – 416Combined sources3
Beta strandi431 – 436Combined sources6
Beta strandi439 – 448Combined sources10
Beta strandi450 – 453Combined sources4
Beta strandi459 – 463Combined sources5
Helixi464 – 467Combined sources4
Helixi468 – 474Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5IX-ray2.90A213-477[»]
ProteinModelPortaliP98119.
SMRiP98119.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98119.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 82Fibronectin type-IPROSITE-ProRule annotationAdd BLAST43
Domaini83 – 121EGF-likePROSITE-ProRule annotationAdd BLAST39
Domaini128 – 209KringlePROSITE-ProRule annotationAdd BLAST82
Domaini226 – 476Peptidase S1PROSITE-ProRule annotationAdd BLAST251

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5IX-ray2.90A213-477[»]
ProteinModelPortaliP98119.
SMRiP98119.
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: November 2, 2016
This is version 113 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.