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   24-JAN-2024, entry version 143.
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   GlyGen; Q6XPR3; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q6XPR3; -.
DR   PhosphoSitePlus; Q6XPR3; -.
DR   BioMuta; RPTN; -.
DR   DMDM; 68566036; -.
DR   MassIVE; Q6XPR3; -.
DR   PaxDb; 9606-ENSP00000317895; -.
DR   PeptideAtlas; Q6XPR3; -.
DR   ProteomicsDB; 67805; -.
DR   Antibodypedia; 34084; 134 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   AGR; HGNC:26809; -.
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; HEDEQNH; -.
DR   OrthoDB; 3936758at2759; -.
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; 14 hits in 1135 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 cell types or tissues.
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   Gene3D; 1.10.238.10; EF-hand; 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; REPETIN; 1.
DR   PANTHER; PTHR14054:SF14; REPETIN; 1.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
DR   Genevisible; Q6XPR3; HS.
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
//