PAMR1_HUMAN
ID PAMR1_HUMAN Reviewed; 720 AA.
AC Q6UXH9; A8MQ58; B7ZA73; Q5EBL7; Q5JPI4; Q6N062; Q71RE9; Q96JW2; Q9Y432;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
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; ORFNames=FP938, UNQ699/PRO1344;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon endothelium, and Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Chondrosarcoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-720 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [7]
RP 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).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
CC -!- FUNCTION: May play a role in regeneration of skeletal muscle.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6UXH9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UXH9-2; Sequence=VSP_025568;
CC Name=3;
CC IsoId=Q6UXH9-3; Sequence=VSP_055371;
CC -!- INDUCTION: Strongly down-regulated in muscle cell lines derived from
CC biopsies of 5 Duchenne muscular dystrophy (DMD) patients compared to a
CC normal muscle cell line. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ15224.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY358346; AAQ88712.1; -; mRNA.
DR EMBL; AK027841; BAB55404.1; -; mRNA.
DR EMBL; AK316188; BAH14559.1; -; mRNA.
DR EMBL; AL050214; CAB43317.1; -; mRNA.
DR EMBL; AL832391; CAI46203.1; -; mRNA.
DR EMBL; BX640676; CAE45808.1; -; mRNA.
DR EMBL; AC090625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089434; AAH89434.1; -; mRNA.
DR EMBL; AF370388; AAQ15224.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31460.1; -. [Q6UXH9-1]
DR CCDS; CCDS60760.1; -. [Q6UXH9-3]
DR CCDS; CCDS7898.1; -. [Q6UXH9-2]
DR PIR; T08805; T08805.
DR RefSeq; NP_001001991.1; NM_001001991.2. [Q6UXH9-1]
DR RefSeq; NP_001269604.1; NM_001282675.1.
DR RefSeq; NP_001269605.1; NM_001282676.1. [Q6UXH9-3]
DR RefSeq; NP_056245.2; NM_015430.3. [Q6UXH9-2]
DR AlphaFoldDB; Q6UXH9; -.
DR SMR; Q6UXH9; -.
DR BioGRID; 117400; 2.
DR IntAct; Q6UXH9; 1.
DR STRING; 9606.ENSP00000482899; -.
DR MEROPS; S01.998; -.
DR GlyGen; Q6UXH9; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q6UXH9; -.
DR PhosphoSitePlus; Q6UXH9; -.
DR BioMuta; PAMR1; -.
DR DMDM; 74738221; -.
DR EPD; Q6UXH9; -.
DR jPOST; Q6UXH9; -.
DR MassIVE; Q6UXH9; -.
DR PaxDb; Q6UXH9; -.
DR PeptideAtlas; Q6UXH9; -.
DR PRIDE; Q6UXH9; -.
DR ProteomicsDB; 1941; -.
DR ProteomicsDB; 67625; -. [Q6UXH9-1]
DR ProteomicsDB; 67626; -. [Q6UXH9-2]
DR Antibodypedia; 25958; 33 antibodies from 14 providers.
DR DNASU; 25891; -.
DR Ensembl; ENST00000615849.4; ENSP00000479260.1; ENSG00000149090.13. [Q6UXH9-3]
DR Ensembl; ENST00000619888.5; ENSP00000483703.1; ENSG00000149090.13. [Q6UXH9-1]
DR Ensembl; ENST00000622144.4; ENSP00000482899.1; ENSG00000149090.13. [Q6UXH9-2]
DR GeneID; 25891; -.
DR KEGG; hsa:25891; -.
DR MANE-Select; ENST00000619888.5; ENSP00000483703.1; NM_001001991.3; NP_001001991.1.
DR UCSC; uc031xjw.2; human. [Q6UXH9-1]
DR CTD; 25891; -.
DR DisGeNET; 25891; -.
DR GeneCards; PAMR1; -.
DR HGNC; HGNC:24554; PAMR1.
DR HPA; ENSG00000149090; Low tissue specificity.
DR neXtProt; NX_Q6UXH9; -.
DR OpenTargets; ENSG00000149090; -.
DR PharmGKB; PA164724339; -.
DR VEuPathDB; HostDB:ENSG00000149090; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000154234; -.
DR InParanoid; Q6UXH9; -.
DR OMA; DIVPCEQ; -.
DR OrthoDB; 267332at2759; -.
DR PhylomeDB; Q6UXH9; -.
DR TreeFam; TF351669; -.
DR PathwayCommons; Q6UXH9; -.
DR SignaLink; Q6UXH9; -.
DR BioGRID-ORCS; 25891; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; PAMR1; human.
DR GenomeRNAi; 25891; -.
DR Pharos; Q6UXH9; Tdark.
DR PRO; PR:Q6UXH9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6UXH9; protein.
DR Bgee; ENSG00000149090; Expressed in decidua and 170 other tissues.
DR ExpressionAtlas; Q6UXH9; baseline and differential.
DR Genevisible; Q6UXH9; HS.
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 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Serine protease homolog; Signal;
KW Sushi.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..720
FT /note="Inactive serine protease PAMR1"
FT /id="PRO_0000287602"
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:0000269|PubMed:16335952"
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 VAR_SEQ 127..238
FT /note="RCGQVLRAPKGQILLESYPLNAHCEWTIHAKPGFVIQLRFVMLSLEFDYMCQ
FT YDYVEVRDGDNRDGQIIKRVCGNERPAPIQSIGSSLHVLFHSDGSKNFDGFHAIYEEIT
FT A -> P (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055371"
FT VAR_SEQ 274
FT /note="L -> LLEAGKSKIKASEDSLSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025568"
FT VARIANT 305
FT /note="A -> T (in dbSNP:rs16927482)"
FT /id="VAR_032335"
FT CONFLICT 257
FT /note="S -> P (in Ref. 2; BAB55404)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="F -> S (in Ref. 2; BAH14559)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="Q -> R (in Ref. 3; CAB43317/CAI46203/CAE45808)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="T -> A (in Ref. 3; CAE45808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 80199 MW; DC898BC7241289D3 CRC64;
MELGCWTQLG LTFLQLLLIS SLPREYTVIN EACPGAEWNI MCRECCEYDQ IECVCPGKRE
VVGYTIPCCR NEENECDSCL IHPGCTIFEN CKSCRNGSWG GTLDDFYVKG FYCAECRAGW
YGGDCMRCGQ VLRAPKGQIL LESYPLNAHC EWTIHAKPGF VIQLRFVMLS LEFDYMCQYD
YVEVRDGDNR DGQIIKRVCG NERPAPIQSI GSSLHVLFHS DGSKNFDGFH AIYEEITACS
SSPCFHDGTC VLDKAGSYKC ACLAGYTGQR CENLLEERNC SDPGGPVNGY QKITGGPGLI
NGRHAKIGTV VSFFCNNSYV LSGNEKRTCQ QNGEWSGKQP ICIKACREPK ISDLVRRRVL
PMQVQSRETP LHQLYSAAFS KQKLQSAPTK KPALPFGDLP MGYQHLHTQL QYECISPFYR
RLGSSRRTCL RTGKWSGRAP SCIPICGKIE NITAPKTQGL RWPWQAAIYR RTSGVHDGSL
HKGAWFLVCS GALVNERTVV VAAHCVTDLG KVTMIKTADL KVVLGKFYRD DDRDEKTIQS
LQISAIILHP NYDPILLDAD IAILKLLDKA RISTRVQPIC LAASRDLSTS FQESHITVAG
WNVLADVRSP GFKNDTLRSG VVSVVDSLLC EEQHEDHGIP VSVTDNMFCA SWEPTAPSDI
CTAETGGIAA VSFPGRASPE PRWHLMGLVS WSYDKTCSHR LSTAFTKVLP FKDWIERNMK
