LOCUS       NP_775773                855 aa            linear   PRI 28-APR-2025
DEFINITION  polyserase-2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_775773
VERSION     NP_775773.2
DBSOURCE    REFSEQ: accession NM_173502.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Cal,S., Quesada,V., Llamazares,M., Diaz-Perales,A., Garabaya,C. and
            Lopez-Otin,C.
  TITLE     Human polyserase-2, a novel enzyme with three tandem serine
            protease domains in a single polypeptide chain
  JOURNAL   J Biol Chem 280 (3), 1953-1961 (2005)
   PUBMED   15536082
  REMARK    GeneRIF: analysis of post-translational processing mechanisms of
            polyserase-2 revealed that this novel polyprotein is a secreted
            enzyme whose three protease domains remain as an integral part of a
            single polypeptide chain
            Erratum:[J Biol Chem. 2018 Jul 27;293(30):11784. doi:
            10.1074/jbc.AAC118.004649. PMID: 30054290]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290310.1, AC009088.9, AK297997.1 and AI864473.1.
            
            On Jan 26, 2005 this sequence version replaced NP_775773.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ627034.1, AK075142.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268281.9/ ENSP00000268281.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..855
                     /product="polyserase-2 isoform 1 precursor"
                     /note="polyserine protease-2; polyserase-2; protease,
                     serine 36"
                     /calculated_mol_wt=89557
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2417
     mat_peptide     47..855
                     /product="Polyserase-2. /id=PRO_0000027880"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5K4E3.2)"
                     /calculated_mol_wt=86975
     Region          47..289
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            47
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(87,139,243)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Site            order(237,262,264)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     Region          292..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Site            317
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Region          330..538
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cl21584"
                     /db_xref="CDD:473915"
     Site            order(363,410,510)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            369
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Site            402
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Site            407
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Site            421
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Site            order(504,529,531)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     Site            508
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5K4E3.2)"
     Region          601..783
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cl21584"
                     /db_xref="CDD:473915"
     CDS             1..855
                     /gene="PRSS36"
                     /coded_by="NM_173502.5:32..2599"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS32436.1"
                     /db_xref="GeneID:146547"
                     /db_xref="HGNC:HGNC:26906"
                     /db_xref="MIM:610560"
ORIGIN      
        1 marhlllplv mlvispipga fqdsalsptq eepedldcgr pepsarivgg snaqpgtwpw
       61 qvslhhgggh icggsliaps wvlsaahcfm tngtlepaae wsvllgvhsq dgpldgahtr
      121 avaaivvpan ysqvelgadl allrlaspas lgpavwpvcl prashrfvhg tacwatgwgd
      181 vqeadplplp wvlqevelrl lgeatcqcly sqpgpfnltl qilpgmlcag ypegrrdtcq
      241 gdsggplvce eggrwfqagi tsfgfgcgrr nrpgvftava tyeawireqv mgsepgpafp
      301 tqpqktqsdp qepreencti alpecgkapr pgawpweaqv mvpgsrpchg alvseswvla
      361 pascfldpns sdspprdlda wrvllpsrpr aervarlvqh enaswdnasd lallqlrtpv
      421 nlsaasrpvc lphpehyflp gsrcrlarwg rgepalgpga lleaellggw wchclygrqg
      481 aavplpgdpp halcpayqek eevgscwnds rwsllcqeeg twflagirdf psgclrpraf
      541 fplqthgpwi shvtrgayle dqlawdwgpd geetetqtcp phtehgacgl rleaapvgvl
      601 wpwlaevhva gdrvctgill apgwvlaath cvlrpgsttv pyievylgra gasslpqghq
      661 vsrlvisirl pqhlglrppl allelssrve pspsalpicl hpagippgas cwvlgwkepq
      721 drvpvaaavs iltqricdcl yqgilppgtl cvlyaegqen rcemtsappl lcqmtegswi
      781 lvgmavqgsr elfaaigpee awisqtvgea nflppsgsph wptggsnlcp pelakasgsp
      841 havyfllllt lliqs
//
