(data stored in ACNUC6881 zone)

HOGENOM: HS3_PE1497

ID   HS3_PE1497                           STANDARD;      PRT;   385 AA.
AC   HS3_PE1497; Q9UI38;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable threonine protease PRSS50; EC=3.4.25 -;AltName:
DE   Full=Cancer/testis antigen 20;AltName: Full=Serine protease 50;AltName:
DE   Full=Testis-specific protease-like protein 50;Flags: Precursor;
DE   (HS3.PE1497).
GN   Name=PRSS50; Synonyms=CT20, TSP50;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS3.PE1497.
CC       Homo sapiens chromosome 3 GRCh37  sequence 1..197962430 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:TSP50_HUMAN
CC   -!- FUNCTION: May be involved in proteolysis through its threonine
CC       endopeptidase activity.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (Probable). Note=May
CC       also localize to cytoplasmic membranes.
CC   -!- TISSUE SPECIFICITY: Testis specific. Differentially expressed in
CC       some breast cancer tissues.
CC   -!- MISCELLANEOUS: DNA hypomethylation is accompanied by the
CC       expression of the gene in the testis.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- CAUTION: Although related to peptidase S1 family, lacks the
CC       conserved active Ser residue in position 310 which is replaced by
CC       a Thr.
CC   -!- GENE_FAMILY: HOG000065742 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000206549;ENST00000315170;ENSP00000326598.
DR   EMBL; AF100707; - ;
DR   EMBL; AK092598; - ;
DR   EMBL; AK097666; - ;
DR   EMBL; BC033016; - ;
DR   EMBL; BC037775; - ;
DR   UniProtKB/Swiss-Prot; Q9UI38; -.
DR   EMBL; AF100707; AAF22500.1; -; mRNA.
DR   EMBL; BC033016; AAH33016.1; -; mRNA.
DR   EMBL; BC037775; AAH37775.1; -; mRNA.
DR   IPI; IPI00002279; -.
DR   RefSeq; NP_037402.1; NM_013270.4.
DR   UniGene; Hs.120365; -.
DR   ProteinModelPortal; Q9UI38; -.
DR   SMR; Q9UI38; 113-362.
DR   STRING; Q9UI38; -.
DR   MEROPS; S01.993; -.
DR   PRIDE; Q9UI38; -.
DR   Ensembl; ENST00000315170; ENSP00000326598; ENSG00000206549.
DR   Ensembl; ENST00000460241; ENSP00000418875; ENSG00000206549.
DR   GeneID; 29122; -.
DR   KEGG; hsa:29122; -.
DR   UCSC; uc003cqe.1; human.
DR   CTD; 29122; -.
DR   GeneCards; GC03M046731; -.
DR   H-InvDB; HIX0017216; -.
DR   HGNC; HGNC:17910; PRSS50.
DR   HPA; CAB008977; -.
DR   MIM; 607950; gene.
DR   neXtProt; NX_Q9UI38; -.
DR   PharmGKB; PA165698443; -.
DR   eggNOG; prNOG16110; -.
DR   GeneTree; ENSGT00600000084189; -.
DR   InParanoid; Q9UI38; -.
DR   OMA; SPWIDQM; -.
DR   OrthoDB; EOG4QFWDF; -.
DR   NextBio; 52221; -.
DR   ArrayExpress; Q9UI38; -.
DR   Bgee; Q9UI38; -.
DR   Genevestigator; Q9UI38; -.
DR   GermOnline; ENSG00000206549; Homo sapiens.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   HOGENOMDNA; HS3.PE1497; -.
KW   ENSG000002065491755old_1320000031; ENSP000003265987901old_1320000031;
KW   B3KS16_HUMAN; B3KUP4_HUMAN; AF100707; AK092598; AK097666; BC033016;
KW   BC037775;
KW   Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Hydrolase; Polymorphism; Protease; Reference proteome;
KW   Serine protease homolog; Signal.
SQ   SEQUENCE   385 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGRWCQTVAR GQRPRTSAPS RAGALLLLLL LLRSAGCWGA GEAPGALSTA DPADQSVQCV
     PKATCPSSRP RLLWQTPTTQ TLPSTTMETQ FPVSEGKVDP YRSCGFSYEQ DPTLRDPEAV
     ARRWPWMVSV RANGTHICAG TIIASQWVLT VAHCLIWRDV IYSVRVGSPW IDQMTQTASD
     VPVLQVIMHS RYRAQRFWSW VGQANDIGLL KLKQELKYSN YVRPICLPGT DYVLKDHSRC
     TVTGWGLSKA DGMWPQFRTI QEKEVIILNN KECDNFYHNF TKIPTLVQII KSQMMCAEDT
     HREKFCYELT GEPLVCSMEG TWYLVGLVSW GAGCQKSEAP PIYLQVSSYQ HWIWDCLNGQ
     ALALPAPSRT LLLALPLPLS LLAAL
//

If you have problems or comments...

PBIL Back to PBIL home page