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MSMP_HUMAN
ID   MSMP_HUMAN              Reviewed;         139 AA.
AC   Q1L6U9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Prostate-associated microseminoprotein;
DE   AltName: Full=PC3-secreted microprotein;
DE   Flags: Precursor;
GN   Name=MSMP; Synonyms=PSMP;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Prostate;
RX   PubMed=17338636; DOI=10.1515/bc.2007.032;
RA   Valtonen-Andre C., Bjartell A., Hellsten R., Lilja H., Haerkoenen P.,
RA   Lundwall A.;
RT   "A highly conserved protein secreted by the prostate cancer cell line PC-3
RT   is expressed in benign and malignant prostate tissue.";
RL   Biol. Chem. 388:289-295(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=24442440; DOI=10.4049/jimmunol.1300758;
RA   Pei X., Sun Q., Zhang Y., Wang P., Peng X., Guo C., Xu E., Zheng Y., Mo X.,
RA   Ma J., Chen D., Zhang Y., Zhang Y., Song Q., Guo S., Shi T., Zhang Z.,
RA   Ma D., Wang Y.;
RT   "PC3-secreted microprotein is a novel chemoattractant protein and functions
RT   as a high-affinity ligand for CC chemokine receptor 2.";
RL   J. Immunol. 192:1878-1886(2014).
CC   -!- FUNCTION: Acts as a ligand for C-C chemokine receptor CCR2
CC       (PubMed:24442440). Signals through binding and activation of CCR2 and
CC       induces a strong chemotactic response and mobilization of intracellular
CC       calcium ions (PubMed:24442440). Exhibits a chemotactic activity for
CC       monocytes and lymphocytes but not neutrophils (PubMed:24442440).
CC       {ECO:0000269|PubMed:24442440}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17338636,
CC       ECO:0000269|PubMed:24442440}.
CC   -!- TISSUE SPECIFICITY: Detected in prostate epithelium (at protein level)
CC       (PubMed:17338636). Detected in trachea and testis (PubMed:17338636).
CC       Highly expressed in benign prostatic hyperplasia and in some prostate
CC       cancers, and can also be detected in breast tumor tissue
CC       (PubMed:17338636, PubMed:24442440). {ECO:0000269|PubMed:17338636,
CC       ECO:0000269|PubMed:24442440}.
CC   -!- SIMILARITY: Belongs to the beta-microseminoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; DQ012170; AAY68208.1; -; mRNA.
DR   EMBL; AL133410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58344.1; -; Genomic_DNA.
DR   CCDS; CCDS43797.1; -.
DR   RefSeq; NP_001037729.1; NM_001044264.2.
DR   AlphaFoldDB; Q1L6U9; -.
DR   SMR; Q1L6U9; -.
DR   BioGRID; 593041; 2.
DR   STRING; 9606.ENSP00000419194; -.
DR   GlyGen; Q1L6U9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q1L6U9; -.
DR   PhosphoSitePlus; Q1L6U9; -.
DR   BioMuta; MSMP; -.
DR   DMDM; 121946765; -.
DR   MassIVE; Q1L6U9; -.
DR   MaxQB; Q1L6U9; -.
DR   PaxDb; Q1L6U9; -.
DR   PeptideAtlas; Q1L6U9; -.
DR   PRIDE; Q1L6U9; -.
DR   ProteomicsDB; 61223; -.
DR   TopDownProteomics; Q1L6U9; -.
DR   Antibodypedia; 56375; 12 antibodies from 7 providers.
DR   DNASU; 692094; -.
DR   Ensembl; ENST00000436428.3; ENSP00000419194.1; ENSG00000215183.5.
DR   GeneID; 692094; -.
DR   KEGG; hsa:692094; -.
DR   MANE-Select; ENST00000436428.3; ENSP00000419194.1; NM_001044264.3; NP_001037729.1.
DR   UCSC; uc003zyb.3; human.
DR   CTD; 692094; -.
DR   DisGeNET; 692094; -.
DR   GeneCards; MSMP; -.
DR   HGNC; HGNC:29663; MSMP.
DR   HPA; ENSG00000215183; Tissue enhanced (brain, choroid plexus, pituitary gland, placenta).
DR   MIM; 612191; gene.
DR   neXtProt; NX_Q1L6U9; -.
DR   OpenTargets; ENSG00000215183; -.
DR   PharmGKB; PA164723190; -.
DR   VEuPathDB; HostDB:ENSG00000215183; -.
DR   eggNOG; ENOG502SBBR; Eukaryota.
DR   GeneTree; ENSGT00940000154371; -.
DR   HOGENOM; CLU_153313_0_0_1; -.
DR   InParanoid; Q1L6U9; -.
DR   OMA; DLEWGSA; -.
DR   OrthoDB; 1429039at2759; -.
DR   PhylomeDB; Q1L6U9; -.
DR   TreeFam; TF338336; -.
DR   PathwayCommons; Q1L6U9; -.
DR   SignaLink; Q1L6U9; -.
DR   BioGRID-ORCS; 692094; 9 hits in 1019 CRISPR screens.
DR   ChiTaRS; MSMP; human.
DR   GenomeRNAi; 692094; -.
DR   Pharos; Q1L6U9; Tdark.
DR   PRO; PR:Q1L6U9; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q1L6U9; protein.
DR   Bgee; ENSG00000215183; Expressed in placenta and 85 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0031727; F:CCR2 chemokine receptor binding; IDA:UniProtKB.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0048247; P:lymphocyte chemotaxis; IDA:UniProtKB.
DR   GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB.
DR   InterPro; IPR008735; PSP94.
DR   PANTHER; PTHR10500; PTHR10500; 1.
DR   Pfam; PF05825; PSP94; 1.
PE   1: Evidence at protein level;
KW   Chemotaxis; Cytokine; Disulfide bond; Inflammatory response;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..139
FT                   /note="Prostate-associated microseminoprotein"
FT                   /id="PRO_0000338648"
FT   REGION          108..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        38..78
FT                   /evidence="ECO:0000250|UniProtKB:P08118"
FT   DISULFID        46..69
FT                   /evidence="ECO:0000250|UniProtKB:P08118"
FT   DISULFID        64..100
FT                   /evidence="ECO:0000250|UniProtKB:P08118"
FT   DISULFID        67..77
FT                   /evidence="ECO:0000250|UniProtKB:P08118"
FT   DISULFID        91..114
FT                   /evidence="ECO:0000250|UniProtKB:P08118"
FT   VARIANT         116
FT                   /note="G -> V (in dbSNP:rs3750436)"
FT                   /id="VAR_043818"
SQ   SEQUENCE   139 AA;  14993 MW;  ED4C9691F0B05E3B CRC64;
     MALRMLWAGQ AKGILGGWGI ICLVMSLLLQ HPGVYSKCYF QAQAPCHYEG KYFTLGESWL
     RKDCFHCTCL HPVGVGCCDT SQHPIDFPAG CEVRQEAGTC QFSLVQKSDP RLPCKGGGPD
     PEWGSANTPV PGAPAPHSS
 
 
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