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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//