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Database: UniProt
Entry: F7DKI4_CALJA
LinkDB: F7DKI4_CALJA
Original site: F7DKI4_CALJA 
ID   F7DKI4_CALJA            Unreviewed;       706 AA.
AC   F7DKI4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 4.
DT   27-MAR-2024, entry version 78.
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:ENSCJAP00000020292.4};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000020292.4, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000020292.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000020292.4}
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   AlphaFoldDB; F7DKI4; -.
DR   Ensembl; ENSCJAT00000021437.4; ENSCJAP00000020292.4; ENSCJAG00000010977.5.
DR   GeneTree; ENSGT00940000154234; -.
DR   HOGENOM; CLU_025988_0_0_1; -.
DR   Proteomes; UP000008225; Chromosome 11.
DR   Bgee; ENSCJAG00000010977; Expressed in liver and 3 other cell types or tissues.
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; IPR001314; Peptidase_S1A.
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   PRINTS; PR00722; CHYMOTRYPSIN.
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:UP000008225};
KW   Serine protease homolog {ECO:0000256|ARBA:ARBA00022542};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}.
FT   DOMAIN          114..222
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          221..258
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          264..330
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          373..430
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          431..706
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        248..257
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        301..328
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   706 AA;  78514 MW;  4A4D8ACF5A016E5D CRC64;
     MSVLLQRHEK EYTVINEACP GAEWNIMCRE CCEYDQIECV CPGKKEVVGY TIPCCRNEEN
     ECDSCLIHPG CTIFENCKSC RNGSWGGTLD DFYVKGFYCA ECRAGWYGGD CMRCGQVLRA
     PKGQILLESY PLNAHCEWTI HAKPGFIIQL RFVMLSLEFD YMCQYDYVEV RDGDNRDSQI
     IKRVCGNERP APVQSTGSSL HVLFHSDGSK NFDGFHAIFE EITACSSSPC FHDGTCVLDK
     AGSYKCACLA GYTGQHCENL LEESNCSDPG VPVNGYKKIT GGPGLINGHS AKIGTIMSFF
     CNNSYVLSGN EKRTCQQNGE WSGKQPICIK ACREPKISDL VRRRVLPMQV QSRETPLHQL
     YSVAFSKQKL QSAPTKKPAL PFGDLPTGYQ HLHTQLQYEC ISPFYRRLGS SRRTCLRTGK
     WSGRAPSCIP ICGKIENVTA LKTQGLRWPW QAAIYRRTSG VHDGGLHKGA WFLICSGALV
     NERTVVVAAH CVTDLGKVTM IKTADLKVVL GKFYRDDDRD EKTIQSLRIS AIILHPNYDP
     ILLDTDIAIL KLLDKARIST GVQPICLAAS RDLSTSFQES HITVAGWNVL ADMRSPGFKN
     DTLRSGVVSV VDSLLCEEQH EDHGIPVSVT DNMFCARQDP AAPSDICTAE TGGIAAVSFP
     GQASLEPRWH LMGLVSWSYD KTCSHILSTA FTKVLLFKDW IERNMK
//
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