PAMR1_PONAB
ID PAMR1_PONAB Reviewed; 720 AA.
AC Q5RDI1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Inactive serine protease PAMR1;
DE AltName: Full=Peptidase domain-containing protein associated with muscle regeneration 1;
DE AltName: Full=Regeneration-associated muscle protease homolog;
DE Flags: Precursor;
GN Name=PAMR1; Synonyms=RAMP;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in regeneration of skeletal muscle.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC active Ser residue in position 665 which is replaced by a Thr,
CC suggesting that it has no protease activity. {ECO:0000305}.
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DR EMBL; CR857928; CAH90176.1; -; mRNA.
DR RefSeq; NP_001125060.1; NM_001131588.1.
DR AlphaFoldDB; Q5RDI1; -.
DR SMR; Q5RDI1; -.
DR STRING; 9601.ENSPPYP00000003852; -.
DR MEROPS; S01.998; -.
DR GeneID; 100171941; -.
DR KEGG; pon:100171941; -.
DR CTD; 25891; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5RDI1; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.290; -; 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 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; SSF49854; SSF49854; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 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 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Serine protease homolog; Signal; Sushi.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..720
FT /note="Inactive serine protease PAMR1"
FT /id="PRO_0000287604"
FT DOMAIN 128..236
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 235..272
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 278..344
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 387..444
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 445..720
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 128..150
FT /evidence="ECO:0000250"
FT DISULFID 177..199
FT /evidence="ECO:0000250"
FT DISULFID 239..250
FT /evidence="ECO:0000250"
FT DISULFID 244..260
FT /evidence="ECO:0000250"
FT DISULFID 262..271
FT /evidence="ECO:0000250"
FT DISULFID 280..329
FT /evidence="ECO:0000250"
FT DISULFID 315..342
FT /evidence="ECO:0000250"
FT DISULFID 414..442
FT /evidence="ECO:0000250"
FT DISULFID 489..505
FT /evidence="ECO:0000250"
FT DISULFID 630..649
FT /evidence="ECO:0000250"
FT DISULFID 661..697
FT /evidence="ECO:0000250"
SQ SEQUENCE 720 AA; 80041 MW; 3F83E2DAD41F4117 CRC64;
MELGCWTQLG LTFLQLLLIS SLPREYTVIN EACPGAEWNI MCRECCEYDQ IECVCPGKKE
VVGYTIPCCR NEENECDSCL IHPGCTIFEN CKSCRNGSWG GTLDDFYVKG FYCAECRAGW
YGGDCMRCGQ VLRAPKGQIL LESYPLNAHC EWTIHAKPGF VIQLRFVMLS LEFDYMCQYD
YVEVRDGDNR DGQIIKRVCG NERPAPIQST GSSLHVLFHS DGSKNFDGFH AIFEEITACS
SSPCFHDGTC VLDKAGSYKC ACLAGYTGQR CENLLEERNC SDPGGPVNGY QKITGGPGLI
NGRHAKIGTV VSFFCNNSYV LSGNEKRTCQ QNGEWSGKQP ICIKACREPK ISDLVRRRVL
PIQVQSRETP LHQLYSAAFS KQKLQSAPTK KPALPFGDLP MGYQHLHTQL QYECISPFYR
RLGSSRRTCL RTGKWSGQAP SCIPICGKIE NVTAPKTQGL RWPWQAAIYR RTSGVHDGSL
HKGAWFLVCS GALVNERTVV VAAHCVTDLG KVTMIKTADL KVILGKFYRD DDRDEKTTQS
LRISAIILHP NYDPILLDAD IAILKLLDKA RISTRVQPIC LAASRDLSTS FQESHITVAG
WNVLADVRSP GFKNDTLRSG VVSVVDSLLC EEQHEDHGIP VSVTDNMFCA SQDPTAPSDI
CTAETGGIAA VSFPGRASPE PRWHLMGLVS WSYDKTCSHR LSTAFTKVLP FKDWIERNMK
