PAMR1_XENTR
ID PAMR1_XENTR Reviewed; 722 AA.
AC Q6DIV5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=F6;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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 667 which is replaced by a Thr,
CC suggesting that it has no protease activity. {ECO:0000305}.
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DR EMBL; BC075430; AAH75430.1; -; mRNA.
DR RefSeq; NP_001004944.1; NM_001004944.1.
DR AlphaFoldDB; Q6DIV5; -.
DR SMR; Q6DIV5; -.
DR STRING; 8364.ENSXETP00000034004; -.
DR MEROPS; S01.998; -.
DR PaxDb; Q6DIV5; -.
DR DNASU; 448349; -.
DR GeneID; 448349; -.
DR KEGG; xtr:448349; -.
DR CTD; 25891; -.
DR Xenbase; XB-GENE-1012813; pamr1.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q6DIV5; -.
DR OrthoDB; 267332at2759; -.
DR PhylomeDB; Q6DIV5; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; 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; -; 2.
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; 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 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..722
FT /note="Inactive serine protease PAMR1"
FT /id="PRO_0000287605"
FT DOMAIN 130..238
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 237..274
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 280..346
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 393..446
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 447..722
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..152
FT /evidence="ECO:0000250"
FT DISULFID 179..201
FT /evidence="ECO:0000250"
FT DISULFID 241..252
FT /evidence="ECO:0000250"
FT DISULFID 246..262
FT /evidence="ECO:0000250"
FT DISULFID 264..273
FT /evidence="ECO:0000250"
FT DISULFID 282..331
FT /evidence="ECO:0000250"
FT DISULFID 317..344
FT /evidence="ECO:0000250"
FT DISULFID 416..444
FT /evidence="ECO:0000250"
FT DISULFID 491..507
FT /evidence="ECO:0000250"
FT DISULFID 632..651
FT /evidence="ECO:0000250"
FT DISULFID 663..699
FT /evidence="ECO:0000250"
SQ SEQUENCE 722 AA; 80367 MW; F173563206D1AE82 CRC64;
MALLVWSSLV VASLHLLGTA AYPSRSKYTV INENCPGAEW NIMCRDCCEY DQVECACPDG
NQKVGYTIPC CRNEENECDS CLIHPGCSIF ENCKSCNNGS WGGTLDDFYI KGSYCSECRM
GWYGGDCMRC GEVIQAARGE IMLESYPFNA RCEWSIQVAP GYTVELRFGM LSLEFDYMCQ
YDYLEVRDGD NVDAKILKRF CGNQRPLSLR STGNSLHLLF QSDGSKNFDG FYVTFEEVTG
CSSTPCFHDG TCIADKTGSY RCACLAGYTG RHCENVIEEK SCKDPGAPMN GYRKLPDGAG
LSLANHIKVG FKIHYFCNNS YVLSGNQERA CLQGAQWSGK QPVCIKACKE PKVADLVRQK
VLPSLVQSRE TPLHQLYSAS FTKEKTDILP TKKPALPPGE LPPGYQHLHT QLQYDCVSPF
YRRTGSSRRT CLKTGKWSGR APSCIPICGK LENFNITQLG EQRWPWQAAL YRRSNGVKDA
SLRKGSWVLV CSGALLNERT VVMAAHCVTD LGKSSIIKVS DMKVVLGKFY RDDDREEKSQ
QHLHISAVIV NPNYDPILLD SDIAVIKLLD KARVSDYVQP VCLTLATEMI TSPQEYTIVI
SGWKILSDPR APGSKNETIR AGAIEPVDSL QCEQQYEENG ISVSVTESMF CAKQEPRPSP
SICPSETGGI TTVLLPSPTS PEGSWHLIGL VSWGYDKSCR KDLYTGYTKV VTFKEWLEKN
MK
