RPTN_HUMAN
ID RPTN_HUMAN Reviewed; 784 AA.
AC Q6XPR3; B7ZBZ3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Repetin;
GN Name=RPTN;
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].
RC TISSUE=Skin;
RA Wu Z., Schroeder J.M.;
RT "Human intermediate filament-associated protein family.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CALCIUM-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=15854042; DOI=10.1111/j.0022-202x.2005.23675.x;
RA Huber M., Siegenthaler G., Mirancea N., Marenholz I., Nizetic D.,
RA Breitkreutz D., Mischke D., Hohl D.;
RT "Isolation and characterization of human repetin, a member of the fused
RT gene family of the epidermal differentiation complex.";
RL J. Invest. Dermatol. 124:998-1007(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
CC -!- FUNCTION: Involved in the cornified cell envelope formation.
CC Multifunctional epidermal matrix protein. Reversibly binds calcium.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Expression is scattered in the normal epidermis but
CC strong in the acrosyringium, the inner hair root sheath and in the
CC filiform papilli of the tongue. {ECO:0000269|PubMed:15854042}.
CC -!- DOMAIN: Can be divided into a N-terminal domain with significant
CC homology to S100-like calcium-binding proteins, a central domain
CC containing a series of short tandem repeats, and two flanking segments
CC with low homology to the consensus sequences of the central repeats.
CC -!- PTM: Potential substrate of transglutaminase. Some arginines are
CC probably converted to citrullines by peptidylarginine deimidase.
CC -!- SIMILARITY: Belongs to the S100-fused protein family. {ECO:0000305}.
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DR EMBL; AY396742; AAR91620.1; -; mRNA.
DR EMBL; AY219924; AAP48705.1; -; Genomic_DNA.
DR EMBL; AL589986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41397.1; -.
DR RefSeq; NP_001116437.1; NM_001122965.1.
DR AlphaFoldDB; Q6XPR3; -.
DR SMR; Q6XPR3; -.
DR BioGRID; 126006; 3.
DR IntAct; Q6XPR3; 4.
DR STRING; 9606.ENSP00000317895; -.
DR iPTMnet; Q6XPR3; -.
DR PhosphoSitePlus; Q6XPR3; -.
DR BioMuta; RPTN; -.
DR DMDM; 68566036; -.
DR MassIVE; Q6XPR3; -.
DR PaxDb; Q6XPR3; -.
DR PeptideAtlas; Q6XPR3; -.
DR PRIDE; Q6XPR3; -.
DR ProteomicsDB; 67805; -.
DR Antibodypedia; 34084; 111 antibodies from 23 providers.
DR DNASU; 126638; -.
DR Ensembl; ENST00000316073.3; ENSP00000317895.3; ENSG00000215853.3.
DR GeneID; 126638; -.
DR KEGG; hsa:126638; -.
DR MANE-Select; ENST00000316073.3; ENSP00000317895.3; NM_001122965.1; NP_001116437.1.
DR UCSC; uc001ezs.1; human.
DR CTD; 126638; -.
DR DisGeNET; 126638; -.
DR GeneCards; RPTN; -.
DR HGNC; HGNC:26809; RPTN.
DR HPA; ENSG00000215853; Tissue enhanced (lymphoid tissue, skin).
DR MIM; 613259; gene.
DR neXtProt; NX_Q6XPR3; -.
DR OpenTargets; ENSG00000215853; -.
DR PharmGKB; PA142670970; -.
DR VEuPathDB; HostDB:ENSG00000215853; -.
DR eggNOG; ENOG502S86J; Eukaryota.
DR GeneTree; ENSGT00940000154467; -.
DR HOGENOM; CLU_010746_0_0_1; -.
DR InParanoid; Q6XPR3; -.
DR OMA; GQTSHYG; -.
DR OrthoDB; 1367189at2759; -.
DR PhylomeDB; Q6XPR3; -.
DR TreeFam; TF338665; -.
DR PathwayCommons; Q6XPR3; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q6XPR3; -.
DR BioGRID-ORCS; 126638; 12 hits in 1059 CRISPR screens.
DR GenomeRNAi; 126638; -.
DR Pharos; Q6XPR3; Tbio.
DR PRO; PR:Q6XPR3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6XPR3; protein.
DR Bgee; ENSG00000215853; Expressed in gingiva and 49 other tissues.
DR Genevisible; Q6XPR3; HS.
DR GO; GO:0001533; C:cornified envelope; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR CDD; cd00213; S-100; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR033198; RPTN.
DR InterPro; IPR034325; S-100_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR14054; PTHR14054; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Calcium; Extracellular matrix; Metal-binding; Reference proteome; Repeat;
KW Secreted.
FT CHAIN 1..784
FT /note="Repetin"
FT /id="PRO_0000144040"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..91
FT /note="S-100-like"
FT /evidence="ECO:0000250"
FT REGION 92..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VARIANT 320
FT /note="S -> G (in dbSNP:rs12117644)"
FT /id="VAR_059177"
SQ SEQUENCE 784 AA; 90731 MW; B4B031B4778EBAA3 CRC64;
MAQLLNSILS VIDVFHKYAK GNGDCALLCK EELKQLLLAE FGDILQRPND PETVETILNL
LDQDRDGHID FHEYLLLVFQ LVQACYHKLD NKSHGGRTSQ QERGQEGAQD CKFPGNTGRQ
HRQRHEEERQ NSHHSQPERQ DGDSHHGQPE RQDRDSHHGQ SEKQDRDSHH SQPERQDRDS
HHNQSERQDK DFSFDQSERQ SQDSSSGKKV SHKSTSGQAK WQGHIFALNR CEKPIQDSHY
GQSERHTQQS ETLGQASHFN QTNQQKSGSY CGQSERLGQE LGCGQTDRQG QSSHYGQTDR
QDQSYHYGQT DRQGQSSHYS QTDRQGQSSH YSQPDRQGQS SHYGQMDRKG QCYHYDQTNR
QGQGSHYSQP NRQGQSSHYG QPDTQDQSSH YGQTDRQDQS SHYGQTERQG QSSHYSQMDR
QGQGSHYGQT DRQGQSSHYG QPDRQGQNSH YGQTDRQGQS SHYGQTDRQG QSSHYSQPDK
QGQSSHYGKI DRQDQSYHYG QPDGQGQSSH YGQTDRQGQS FHYGQPDRQG QSSHYSQMDR
QGQSSHYGQT DRQGQSSHYG QTDRQGQSYH YGQTDRQGQS SHYIQSQTGE IQGQNKYFQG
TEGTRKASYV EQSGRSGRLS QQTPGQEGYQ NQGQGFQSRD SQQNGHQVWE PEEDSQHHQH
KLLAQIQQER PLCHKGRDWQ SCSSEQGHRQ AQTRQSHGEG LSHWAEEEQG HQTWDRHSHE
SQEGPCGTQD RRTHKDEQNH QRRDRQTHEH EQSHQRRDRQ THEDKQNRQR RDRQTHEDEQ
NHQR
