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Database: UniProt
Entry: K7FU61_PELSI
LinkDB: K7FU61_PELSI
Original site: K7FU61_PELSI 
ID   K7FU61_PELSI            Unreviewed;       723 AA.
AC   K7FU61;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Inactive serine protease PAMR1 {ECO:0000256|ARBA:ARBA00040464};
DE   AltName: Full=Peptidase domain-containing protein associated with muscle regeneration 1 {ECO:0000256|ARBA:ARBA00042985};
DE   AltName: Full=Regeneration-associated muscle protease homolog {ECO:0000256|ARBA:ARBA00041872};
GN   Name=PAMR1 {ECO:0000313|Ensembl:ENSPSIP00000011571.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000011571.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000011571.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role in regeneration of skeletal muscle.
CC       {ECO:0000256|ARBA:ARBA00037622}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; AGCU01095516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01095517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01095518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01095519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01095520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K7FU61; -.
DR   STRING; 13735.ENSPSIP00000011571; -.
DR   Ensembl; ENSPSIT00000011628.1; ENSPSIP00000011571.1; ENSPSIG00000010368.1.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000154234; -.
DR   OMA; YCAECRG; -.
DR   TreeFam; TF351669; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24254:SF9; INACTIVE SERINE PROTEASE PAMR1; 1.
DR   PANTHER; PTHR24254; PROTHROMBIN; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW   Serine protease homolog {ECO:0000256|ARBA:ARBA00022542};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT   DOMAIN          131..239
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          238..275
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          281..347
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          392..447
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          448..723
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        265..274
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        318..345
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   723 AA;  80798 MW;  74A00584066B54AC CRC64;
     TDLSIWTLHS PSSMKCLIFP SPDFLFLEYT VINENCPGAE WNIMCRECCE YDQIQCVCPG
     GKEKVGYTIP CCRNEENECD SCLIHPGCTI FENCKSCRNG SWGGTLDDFY IKGIYCAACR
     AGWYGGDCMS CGQVLQASKG QILLESYPLN AHCEWTIHVK PGFSIELRFA MLSLEFDYMC
     QYDYVEIRDG DNVDSRIIKR FCGNDRPPPI RSTGTSLHVL FQSDGSKNFD GFHAIFEEIT
     ACSSSPCFHD GTCILDKAGA YRCACLAGYT GNHCESFLHE KNCSDPGGPF NGYRKVVEDT
     GLMNGRYAKI GTVIAFFCNN SYVLSGNEQR TCQDNGEWSG KQPICIKACR EPKISDLVRQ
     KVLPMQVQSR ETPLHQLYSS AFSKQKLEVY PTKKPMLPFG DLPPGYQHLH TQLKYDCISP
     FYRRLGSSRR TCLKSGKWSG RAPSCVPICG KAENITLQKT SSIRWPWQAA IYRKANGVKE
     VSLRKGAWIL ICSGALVNER TVVVAAHCVT DLGKITVLKT ADLKVVLGKF YRDDDRNEKT
     IQNLRISAII VHPNYDPILL DSDMAIIKLL DKAKISSHVQ PICLASAHDL DPSTEDLKIV
     ITGWKILADV KDPSYKNDTI RMGAVQMVDS LLCEQKYEDN GIQVIITDSM FCARQHPTAF
     SNICPAETGG IAAITLPGKA SPELKWHLMG LVSWGDDKTC SLELYTGYTK AIPFKDWIEK
     NMK
//
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