ID A0A2K6M0R6_RHIBE Unreviewed; 720 AA.
AC A0A2K6M0R6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSRBIP00000029368.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000029368.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000029368.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000029368.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_017705233.1; XM_017849744.1.
DR AlphaFoldDB; A0A2K6M0R6; -.
DR Ensembl; ENSRBIT00000053318.1; ENSRBIP00000029368.1; ENSRBIG00000038564.1.
DR GeneID; 108513840; -.
DR CTD; 25891; -.
DR GeneTree; ENSGT00940000154234; -.
DR OMA; YCAECRG; -.
DR OrthoDB; 3547215at2759; -.
DR Proteomes; UP000233180; Unplaced.
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; 2.
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:UP000233180};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..720
FT /note="Inactive serine protease PAMR1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014351467"
FT DOMAIN 128..236
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 235..272
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 278..344
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 387..444
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 445..720
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 262..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 315..342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 720 AA; 80066 MW; F4F55273CF20C2EB CRC64;
MELGCWTQLG LTFLQLLLIS SLPREYTVIN EACPGAEWNI MCRECCEYDQ IECVCPGKKE
VVGYTIPCCR NEENECDSCL IHPGCTIFEN CKSCRNGSWG GTLDDFYVKG FYCAECRAGW
YGGDCMRCGQ VLRAPKGQIL LESYPLNSHC EWTIHAKPGF IIQLRFVMLS LEFDYMCQYD
YVEVRDGDNR DGQIIKRVCG NERPAPIQST GSSLHVLFHS DGSKNFDGFH AIFEEITACS
SSPCFHDGTC VLDKAGSYKC ACLAGYTGQH CENLLEERNC SDPGGPVNGY KKITGGPGLI
NGRHAKIGTV VSFFCNNSYV LSGNEKRTCQ QNGEWSGKQP ICIKACREPK ISDLVRRRVL
PMQVQSRETP LHQLYSAAFS KQKLQSAPTK KPALPFGDLP TGYQHLHTQL QYECISPFYR
RLGSSRRTCL RTGKWSGRAP SCIPICGKIE NVTAPKTQGL RWPWQAAIYR RTSGVHDGSL
HKGAWFLVCS GALVNERTVV VAAHCVTDLG KVTMIKTADL KVVLGKFYRD DDRDEKTIQS
LRISAIILHP NYDPILLDAD IAILKLLDKA RISTRVQPIC LAASRDLSTS FQESHITVAG
WNVLADVRSP GFKNDTLRSG VVSVVDSLLC EEQHEDHGIP VSVTDNMFCA SQDPTAPSDI
CTAETGGIAA VSFPGRASPE PRWHLMGLVS WSYDKTCSHR LSTAFTKVLP FKDWIERNMK
//
