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
//