RPTN_MOUSE
ID RPTN_MOUSE Reviewed; 1118 AA.
AC P97347; G3X968;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Repetin;
GN Name=Rptn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DOMAIN.
RC STRAIN=NMRI; TISSUE=Skin;
RX PubMed=9268637; DOI=10.1006/geno.1997.4818;
RA Krieg P., Schuppler M., Koesters R., Mincheva A., Lichter P., Marks F.;
RT "Repetin (Rptn), a new member of the 'fused gene' subgroup within the S100
RT gene family encoding a murine epidermal differentiation protein.";
RL Genomics 43:339-348(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the cornified cell envelope formation.
CC Multifunctional epidermal matrix protein.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detectable in the stratified internal epithelia of
CC forestomach and tongue and to a lesser degree in normal skin epidermis,
CC where it is restricted to the differentiated suprabasal cell layers.
CC Overexpressed in skin tumors. {ECO:0000269|PubMed:9268637}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late differentiation of the
CC epidermis. {ECO:0000269|PubMed:9268637}.
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 {ECO:0000269|PubMed:9268637}.
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; X99251; CAA67624.1; -; Genomic_DNA.
DR EMBL; AC123859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466656; EDL00666.1; -; Genomic_DNA.
DR CCDS; CCDS17581.1; -.
DR PIR; T30251; T30251.
DR RefSeq; NP_033126.2; NM_009100.2.
DR AlphaFoldDB; P97347; -.
DR SMR; P97347; -.
DR STRING; 10090.ENSMUSP00000044998; -.
DR iPTMnet; P97347; -.
DR PhosphoSitePlus; P97347; -.
DR MaxQB; P97347; -.
DR PaxDb; P97347; -.
DR PRIDE; P97347; -.
DR ProteomicsDB; 299880; -.
DR Antibodypedia; 34084; 111 antibodies from 23 providers.
DR DNASU; 20129; -.
DR Ensembl; ENSMUST00000045912; ENSMUSP00000044998; ENSMUSG00000041984.
DR GeneID; 20129; -.
DR KEGG; mmu:20129; -.
DR UCSC; uc008qfh.1; mouse.
DR CTD; 126638; -.
DR MGI; MGI:1099055; Rptn.
DR VEuPathDB; HostDB:ENSMUSG00000041984; -.
DR eggNOG; ENOG502S86J; Eukaryota.
DR GeneTree; ENSGT00940000154467; -.
DR HOGENOM; CLU_010746_0_0_1; -.
DR InParanoid; P97347; -.
DR OMA; PHQGQKG; -.
DR OrthoDB; 1367189at2759; -.
DR PhylomeDB; P97347; -.
DR TreeFam; TF338665; -.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 20129; 3 hits in 71 CRISPR screens.
DR PRO; PR:P97347; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P97347; protein.
DR Bgee; ENSMUSG00000041984; Expressed in esophagus and 39 other tissues.
DR Genevisible; P97347; MM.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
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; 5.
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 2: Evidence at transcript level;
KW Calcium; Extracellular matrix; Metal-binding; Reference proteome; Repeat;
KW Secreted.
FT CHAIN 1..1118
FT /note="Repetin"
FT /id="PRO_0000144041"
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 REPEAT 273..284
FT /note="1-1"
FT REPEAT 285..296
FT /note="1-2"
FT REPEAT 297..308
FT /note="1-3"
FT REPEAT 309..320
FT /note="1-4"
FT REPEAT 321..332
FT /note="2-1"
FT REPEAT 333..344
FT /note="2-2"
FT REPEAT 345..356
FT /note="2-3"
FT REPEAT 357..368
FT /note="2-4"
FT REPEAT 369..380
FT /note="2-5"
FT REPEAT 381..392
FT /note="2-6"
FT REPEAT 393..404
FT /note="2-7"
FT REPEAT 405..416
FT /note="2-8"
FT REPEAT 417..428
FT /note="2-9"
FT REPEAT 429..440
FT /note="2-10"
FT REPEAT 441..452
FT /note="2-11"
FT REPEAT 453..464
FT /note="2-12"
FT REPEAT 465..476
FT /note="2-13"
FT REPEAT 477..488
FT /note="1-5"
FT REPEAT 489..500
FT /note="1-6"
FT REPEAT 501..512
FT /note="1-7"
FT REPEAT 513..524
FT /note="1-8"
FT REPEAT 525..536
FT /note="1-9"
FT REPEAT 537..548
FT /note="1-10"
FT REPEAT 549..560
FT /note="1-11"
FT REPEAT 561..572
FT /note="1-12"
FT REPEAT 573..584
FT /note="1-13"
FT REPEAT 585..596
FT /note="1-14"
FT REPEAT 597..608
FT /note="1-15"
FT REPEAT 609..620
FT /note="1-16"
FT REPEAT 621..632
FT /note="1-17"
FT REPEAT 633..644
FT /note="1-18"
FT REPEAT 645..656
FT /note="1-19"
FT REPEAT 657..668
FT /note="2-14"
FT REPEAT 669..680
FT /note="2-15"
FT REPEAT 681..692
FT /note="2-16"
FT REPEAT 693..704
FT /note="2-17"
FT REPEAT 705..716
FT /note="2-18"
FT REPEAT 717..728
FT /note="2-19"
FT REPEAT 729..740
FT /note="2-20"
FT REPEAT 741..752
FT /note="2-21"
FT REPEAT 753..764
FT /note="2-22"
FT REPEAT 765..776
FT /note="1-20"
FT REPEAT 777..788
FT /note="1-21"
FT REPEAT 789..800
FT /note="1-22"
FT REPEAT 801..812
FT /note="1-23"
FT REPEAT 813..824
FT /note="1-24"
FT REPEAT 825..836
FT /note="1-25"
FT REPEAT 837..848
FT /note="1-26"
FT REGION 1..91
FT /note="S-100-like"
FT REGION 94..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..848
FT /note="48 X 12 AA approximate tandem repeats of Q-[KT]-
FT [GD]-[RS]-Q-[DG]-Q-S-[PS]-H-X-G"
FT REGION 321..764
FT /note="22 X 12 AA approximate tandem repeats of Q-K-G-R-Q-
FT D-Q-S-P-H-Q-G"
FT COMPBIAS 94..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
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 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 CONFLICT 505..506
FT /note="HS -> QG (in Ref. 1; CAA67624)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="S -> SSHQGQKGRQDLS (in Ref. 1; CAA67624)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="D -> E (in Ref. 1; CAA67624)"
FT /evidence="ECO:0000305"
FT CONFLICT 878
FT /note="Q -> H (in Ref. 1; CAA67624)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="V -> G (in Ref. 1; CAA67624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1118 AA; 128619 MW; 8ADA3117825C125F CRC64;
MPQLLNSILN VSKVFQDYAE YHGVGASLSK KELKQLLLTE FGDILRRPND PETVETILEH
LDRDRNGYVD FHEYLLLVFQ LVQACHHKLD SKFYGSRTSS QKEHDQEGTR SHKFSESTGR
QHRQRYEGER RNSHHNQSEG QHQNVQHDQS QRQDKDSERH DTDPHCGQSE TFHGDSHYGH
SERQDTDYSS DQSESDNESS SSSQRLGYKS SHEQPKGQGY VFALSQSKNP EQAFHYGQSK
TSGQQSSHGQ SGRFRKDSYS SQTSQQESDS YEQYGSQHQK SGNSQTERQG QNSQYGQTNK
KGHSSYHEQT EGQGQSFHYG QKGRKDQSFQ QGQKGRKDQS PHLGQKGRQD QSPHRGQKGR
QDQSPHQGQK GRQDQSPHRG QKGRQDQSPH QGQKGRQDQS PHLGQKGRQD QSPHQGQKGR
QDQSPHQGQK GRQDQSSHQG QKGRQDQSSH QGQKGRQDQS SHQGQKGRQD QSSHQGQREG
QDQNSQWHRT DSQGQSFHYG QTGGHSLSSH QGQTDSQGQN SNWHRTDSQG QSFHYGQTGG
QGLSSHQGQT DSQGQNSNWH RTDSQGQSFH FDQAGREVQG SHHGQTDRQS QNSNWHRTDS
QGQSFHFDQA GKEVQGSHQG QTDSQGQSSH WHQTDRQGQS SQQGHKDRQG QNTHQGQKGR
QDLSPHQGQK GRQDQSPHLG QKGRHDQSPH QGQKGRHDQS PHQGQKGRQD LSSHQGQKGR
QDQSPHLGQK GRHDQSPHRG QKGRQDQSPH QGQKGRQDQS SHQGQREGQD QNSHWHRTDR
QGQSFHYGQT GGQGLSSHQG QTDSQGQNSQ WHRTDSQGQS FHFDQAGREG QSSHHGQTDR
QSQSSHCGQS EIGKTENQGQ NRHSLGTDRT RRDSYVEQSG RSVKLSQQNS REEVRQTQSQ
RSHDRREQQI QQQTWKPKED NQHKLLAQVQ QEPYSYEEYD WQSQSSEQDH CGEEEYQDWD
RHSVEDQENL YEMQNWQTHE EEQSHQTSDR QTHVDEQNQQ RQHRQTHEEN HDHQHGRHHE
DEHNHRRQDH HQQRERQTHE EKEKYQGGQD QSRSFPNREK SHMSEDDQCE GPQGRRFHPT
HGGGKSQRRE KSGNHPTKPA NYSSPLYDYV QEQAAYQY
