PAMR1_BOVIN
ID PAMR1_BOVIN Reviewed; 720 AA.
AC Q5E9P5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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}.
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; BT020875; AAX08892.1; -; mRNA.
DR EMBL; BT029795; ABM06063.1; -; mRNA.
DR RefSeq; NP_001015591.1; NM_001015591.1.
DR AlphaFoldDB; Q5E9P5; -.
DR SMR; Q5E9P5; -.
DR STRING; 9913.ENSBTAP00000016767; -.
DR MEROPS; S01.998; -.
DR PaxDb; Q5E9P5; -.
DR GeneID; 513841; -.
DR KEGG; bta:513841; -.
DR CTD; 25891; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5E9P5; -.
DR OrthoDB; 267332at2759; -.
DR Proteomes; UP000009136; 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_0000287601"
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 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; 80057 MW; 69DA098FF95037E1 CRC64;
MELGWWPQLG LAFLQLLLIS SLPREYTVIN EACPGAEWNI MCRECCEYDQ IKCECPGKKE
VVGYTIPCCR NEENECDSCL IHPGCTIFEN CKTCRNGSWG GTLDDFYVKG IYCAECRAGW
YGGDCMRCGQ VLRVPKGQIL LESYPLNAHC EWTIHAKPGF IIQLRIVMLS LEFDYMCQYD
YVEVRDGDSS DSQIIKRFCG NERPAPIRST GSSLHILFHS DGSKNFDGFH AIFEEITACS
SSPCFHDGTC LLDSTGSYKC ACLAGYTGKH CENLLEERNC SDPGGPVNGY KKITGGPGLI
HGHYAKIGTV LTFFCNSSYV LSGNEMRTCQ QNGEWSGKQP ICIKACREPK ISDLVRRKVL
PMQVQSRETP LHQLYSSAFS KQKLQDAPTK KPVLPFGDLP PGYQHLHTQL QYECISPFYR
RLGSSRRTCL RTGKWSGRAP SCIPICGKTE NVSAPKTQGT RWPWQAAIYR RAGGVHGGGL
HKDAWFLVCS GALVNERTVV VAAHCVTDLG RVTVIKTADL KVVLGKFYRD DDRDEKSIQS
LRISAIILHP NYDPILLDMD IAILKLLDKA RMSTRVQPIC LAAPRDLSTS FQESRITVAG
WNVLADSRSP GYKDDMLRSG VVRVADSLLC EEQHEAQGIP VSVTDSMFCA GRDPTAPSDI
CTAETGGIAA VSFPGRASPE PRWHLVGLVS WSYDKTCSHS LSTAFTKVLP FKDWIERNMK
