PAMR1_MOUSE
ID PAMR1_MOUSE Reviewed; 720 AA.
AC Q8BU25; A2AQI2; Q8K2B8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 143.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP POSSIBLE FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15111323; DOI=10.1016/s0002-9440(10)63735-2;
RA Nakayama Y., Nara N., Kawakita Y., Takeshima Y., Arakawa M., Katoh M.,
RA Morita S., Iwatsuki K., Tanaka K., Okamoto S., Kitamura T., Seki N.,
RA Matsuda R., Matsuo M., Saito K., Hara T.;
RT "Cloning of cDNA encoding a regeneration-associated muscle protease whose
RT expression is attenuated in cell lines derived from Duchenne muscular
RT dystrophy patients.";
RL Am. J. Pathol. 164:1773-1782(2004).
CC -!- FUNCTION: May play a role in regeneration of skeletal muscle.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in normal skeletal muscle
CC and brain. Expression is enhanced in the regenerating area of injured
CC skeletal muscle in mice. {ECO:0000269|PubMed:15111323}.
CC -!- INDUCTION: Down-regulated in dystrophin-mutant mdx muscle cell line.
CC {ECO:0000269|PubMed:15111323}.
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; AK088017; BAC40098.1; -; mRNA.
DR EMBL; AL844605; CAM27621.1; -; Genomic_DNA.
DR EMBL; AL845276; CAM27621.1; JOINED; Genomic_DNA.
DR EMBL; CH466519; EDL27671.1; -; Genomic_DNA.
DR EMBL; BC031841; AAH31841.1; -; mRNA.
DR EMBL; BC057685; AAH57685.1; -; mRNA.
DR CCDS; CCDS16468.1; -.
DR RefSeq; NP_776110.3; NM_173749.4.
DR AlphaFoldDB; Q8BU25; -.
DR SMR; Q8BU25; -.
DR STRING; 10090.ENSMUSP00000028612; -.
DR GlyConnect; 2390; 1 N-Linked glycan (1 site).
DR GlyGen; Q8BU25; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BU25; -.
DR PhosphoSitePlus; Q8BU25; -.
DR MaxQB; Q8BU25; -.
DR PaxDb; Q8BU25; -.
DR PRIDE; Q8BU25; -.
DR ProteomicsDB; 294378; -.
DR Antibodypedia; 25958; 33 antibodies from 14 providers.
DR DNASU; 210622; -.
DR Ensembl; ENSMUST00000028612; ENSMUSP00000028612; ENSMUSG00000027188.
DR GeneID; 210622; -.
DR KEGG; mmu:210622; -.
DR UCSC; uc012caf.1; mouse.
DR CTD; 25891; -.
DR MGI; MGI:2445082; Pamr1.
DR VEuPathDB; HostDB:ENSMUSG00000027188; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000154234; -.
DR HOGENOM; CLU_025988_0_0_1; -.
DR InParanoid; Q8BU25; -.
DR OMA; DIVPCEQ; -.
DR OrthoDB; 267332at2759; -.
DR PhylomeDB; Q8BU25; -.
DR TreeFam; TF351669; -.
DR BioGRID-ORCS; 210622; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Pamr1; mouse.
DR PRO; PR:Q8BU25; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BU25; protein.
DR Bgee; ENSMUSG00000027188; Expressed in body wall and 229 other tissues.
DR Genevisible; Q8BU25; MM.
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_0000287603"
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 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"
FT CONFLICT 114
FT /note="A -> E (in Ref. 4; AAH31841/AAH57685)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="R -> H (in Ref. 1; BAC40098)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 80320 MW; 845BC9660EC4FE3C CRC64;
MELDRWAQLG LVFLQLLLIS SLPREYTVIN EACPGAEWNI MCRECCEYDQ IECLCPGKKE
VVGYTIPCCR NEDNECDSCL IHPGCTIFEN CKSCRNGSWG GTLDDFYVKG FYCAECRAGW
YGGDCMRCGQ VLRASKGQIL LESYPLNAHC EWTIHARPGF IIQLRFGMLS LEFDYMCQYD
YVEVRDGDNS DSPIIKRFCG NERPAPIRST GSSLHVLFHS DGSKNFDGFH AVFEEITACS
SSPCFHDGTC LLDTTGSFKC ACLAGYTGQR CENLLEERNC SDLGGPVNGY KKITEGPGLL
NERHVKIGTV VSFFCNGSYV LSGNEKRTCQ QNGEWSGKQP VCMKACREPK ISDLVRRRVL
SMQVQSRETP LHQLYSTAFS KQKLQDASTK KPALPFGDLP PGYQHLHTQV QYECISPFYR
RLGSSRRTCL RTGKWSGRAP SCIPICGKIE STPSPKTQGT RWPWQAAIYR RTSGVHDGGL
HKGAWFLVCS GALVNERTVV VAAHCVTELG KATIIKTADL KVVLGKFYRD DDRDEKSIQN
LRVSAIILHP NYDPILLDTD IAVLKLLDKA RISTRVQPIC LATTRDLSTS FQESHITVAG
WNILADVRSP GFKNDTLHYG MVRVVDPMLC EEQHEDHGIP VSVTDNMFCA SKDPSTPSDI
CTAETGGIAA LSFPGRASPE PRWHLVGLVS WSYDKTCSNG LSTAFTKVLP FKDWIERNMK
