位置:首页 > 蛋白库 > PRS35_HUMAN
PRS35_HUMAN
ID   PRS35_HUMAN             Reviewed;         413 AA.
AC   Q8N3Z0; A8K7B3; Q9BQP6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Inactive serine protease 35;
DE   Flags: Precursor;
GN   Name=PRSS35; Synonyms=C6orf158; ORFNames=UNQ522/PRO1057;
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], AND VARIANT GLN-224.
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], AND VARIANT GLN-224.
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 GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-224.
RC   TISSUE=Brain;
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).
CC   -!- INTERACTION:
CC       Q8N3Z0; Q07021: C1QBP; NbExp=4; IntAct=EBI-20628340, EBI-347528;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
CC   -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC       active Ser residue in position 346 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; AY358661; AAQ89024.1; -; mRNA.
DR   EMBL; AK291928; BAF84617.1; -; mRNA.
DR   EMBL; AL121939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48663.1; -; Genomic_DNA.
DR   EMBL; BC037170; AAH37170.1; -; mRNA.
DR   CCDS; CCDS4999.1; -.
DR   RefSeq; NP_001163894.1; NM_001170423.1.
DR   RefSeq; NP_699193.2; NM_153362.2.
DR   AlphaFoldDB; Q8N3Z0; -.
DR   BioGRID; 127949; 6.
DR   IntAct; Q8N3Z0; 32.
DR   STRING; 9606.ENSP00000358714; -.
DR   MEROPS; S01.994; -.
DR   GlyGen; Q8N3Z0; 1 site.
DR   iPTMnet; Q8N3Z0; -.
DR   PhosphoSitePlus; Q8N3Z0; -.
DR   BioMuta; PRSS35; -.
DR   DMDM; 158563845; -.
DR   MassIVE; Q8N3Z0; -.
DR   PaxDb; Q8N3Z0; -.
DR   PeptideAtlas; Q8N3Z0; -.
DR   PRIDE; Q8N3Z0; -.
DR   ProteomicsDB; 71852; -.
DR   TopDownProteomics; Q8N3Z0; -.
DR   Antibodypedia; 31685; 82 antibodies from 19 providers.
DR   DNASU; 167681; -.
DR   Ensembl; ENST00000369700.4; ENSP00000358714.3; ENSG00000146250.7.
DR   GeneID; 167681; -.
DR   KEGG; hsa:167681; -.
DR   MANE-Select; ENST00000369700.4; ENSP00000358714.3; NM_153362.3; NP_699193.2.
DR   UCSC; uc003pjz.4; human.
DR   CTD; 167681; -.
DR   DisGeNET; 167681; -.
DR   GeneCards; PRSS35; -.
DR   HGNC; HGNC:21387; PRSS35.
DR   HPA; ENSG00000146250; Tissue enriched (retina).
DR   neXtProt; NX_Q8N3Z0; -.
DR   OpenTargets; ENSG00000146250; -.
DR   PharmGKB; PA134974089; -.
DR   VEuPathDB; HostDB:ENSG00000146250; -.
DR   eggNOG; ENOG502QV0K; Eukaryota.
DR   GeneTree; ENSGT00390000000155; -.
DR   HOGENOM; CLU_055829_0_0_1; -.
DR   InParanoid; Q8N3Z0; -.
DR   OMA; MEQDFMW; -.
DR   OrthoDB; 1245017at2759; -.
DR   PhylomeDB; Q8N3Z0; -.
DR   TreeFam; TF329011; -.
DR   PathwayCommons; Q8N3Z0; -.
DR   SignaLink; Q8N3Z0; -.
DR   BioGRID-ORCS; 167681; 15 hits in 1069 CRISPR screens.
DR   GenomeRNAi; 167681; -.
DR   Pharos; Q8N3Z0; Tbio.
DR   PRO; PR:Q8N3Z0; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q8N3Z0; protein.
DR   Bgee; ENSG00000146250; Expressed in tibia and 128 other tissues.
DR   Genevisible; Q8N3Z0; HS.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   Pfam; PF00089; Trypsin; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Serine protease homolog; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..413
FT                   /note="Inactive serine protease 35"
FT                   /id="PRO_0000299358"
FT   DOMAIN          124..408
FT                   /note="Peptidase S1"
FT   REGION          191..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..206
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        154..170
FT                   /evidence="ECO:0000250"
FT   VARIANT         224
FT                   /note="R -> Q (in dbSNP:rs504593)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_034810"
SQ   SEQUENCE   413 AA;  47098 MW;  818D9C951BD2D6C1 CRC64;
     MENMLLWLIF FTPGWTLIDG SEMEWDFMWH LRKVPRIVSE RTFHLTSPAF EADAKMMVNT
     VCGIECQKEL PTPSLSELED YLSYETVFEN GTRTLTRVKV QDLVLEPTQN ITTKGVSVRR
     KRQVYGTDSR FSILDKRFLT NFPFSTAVKL STGCSGILIS PQHVLTAAHC VHDGKDYVKG
     SKKLRVGLLK MRNKSGGKKR RGSKRSRREA SGGDQREGTR EHLRERAKGG RRRKKSGRGQ
     RIAEGRPSFQ WTRVKNTHIP KGWARGGMGD ATLDYDYALL ELKRAHKKKY MELGISPTIK
     KMPGGMIHFS GFDNDRADQL VYRFCSVSDE SNDLLYQYCD AESGSTGSGV YLRLKDPDKK
     NWKRKIIAVY SGHQWVDVHG VQKDYNVAVR ITPLKYAQIC LWIHGNDANC AYG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024