TRHY_RABIT
ID TRHY_RABIT Reviewed; 1407 AA.
AC P37709;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Trichohyalin;
GN Name=TCHH; Synonyms=THH;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fietz M.J., Rogers G.E.;
RT "Examination of the gene encoding rabbit trichohyalin.";
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Intermediate filament-associated protein that associates in
CC regular arrays with keratin intermediate filaments (KIF) of the inner
CC root sheath cells of the hair follicle and the granular layer of the
CC epidermis. It later becomes cross-linked to KIF by isodipeptide bonds.
CC It may serve as scaffold protein, together with involucrin, in the
CC organization of the cell envelope or even anchor the cell envelope to
CC the KIF network. It may be involved in its own calcium-dependent
CC postsynthetic processing during terminal differentiation.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Found in the hard keratinizing tissues such as the
CC inner root sheath (IRS) of hair follicles and medulla, and in the
CC filiform papillae of dorsal tongue epithelium.
CC -!- DEVELOPMENTAL STAGE: Expressed during late differentiation of the
CC epidermis.
CC -!- DOMAIN: Consists of nine domains. Domain 1 contains two EF-hand
CC calcium-binding domains. Domains 2-4, 6, and 8 are almost entirely
CC alpha-helical, configured as a series of peptide repeats of varying
CC regularity, and are thought to form a single-stranded alpha-helical rod
CC stabilized by ionic interactions. Domain 6 is the most regular and may
CC bind KIF directly by ionic interactions. Domains 5 and 7 are less well
CC organized and may induce folds in the molecule. Domain 9 contains the
CC C-terminus, conserved among different species.
CC -!- PTM: Substrate of transglutaminase. Some 200 arginines are probably
CC converted to citrullines by peptidylarginine deimidase.
CC -!- SIMILARITY: Belongs to the S100-fused protein family. {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; Z19092; CAA79519.1; -; Genomic_DNA.
DR PIR; S28589; S28589.
DR AlphaFoldDB; P37709; -.
DR SMR; P37709; -.
DR STRING; 9986.ENSOCUP00000004511; -.
DR PRIDE; P37709; -.
DR eggNOG; ENOG502QQH0; Eukaryota.
DR InParanoid; P37709; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0045109; P:intermediate filament organization; IEA:InterPro.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
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; IPR034325; S-100_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR033200; TCHH.
DR PANTHER; PTHR34855; PTHR34855; 7.
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; Citrullination; Keratinization; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..1407
FT /note="Trichohyalin"
FT /id="PRO_0000144043"
FT DOMAIN 23..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 REGION 148..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1376
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 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"
SQ SEQUENCE 1407 AA; 183781 MW; AE17D2A159F12B7F CRC64;
MSPLLKSIID IIEIFNQYAS HDCDGAVLKK KDLKILLDRE FGAVLQRPHD PETVDVMLEL
LDRDSDGLVG FDEFCLLIFK LAQAAYYALG QASGLDEEKR SHGEGKGRLL QNRRQEDQRR
FELRDRQFED EPERRRWQKQ EQERELAEEE EQRKKRERFE QHYSRQYRDK EQRLQRQELE
ERRAEEEQLR RRKGRDAEEF IEEEQLRRRE QQELKRELRE EEQQRRERRE QHERALQEEE
EQLLRQRRWR EEPREQQQLR RELEEIRERE QRLEQEERRE QQLRREQRLE QEERREQQLR
RELEEIRERE QRLEQEERRE QRLEQEERRE QQLKRELEEI REREQRLEQE ERREQLLAEE
VREQARERGE SLTRRWQRQL ESEAGARQSK VYSRPRRQEE QSLRQDQERR QRQERERELE
EQARRQQQWQ AEEESERRRQ RLSARPSLRE RQLRAEERQE QEQRFREEEE QRRERRQELQ
FLEEEEQLQR RERAQQLQEE DSFQEDRERR RRQQEQRPGQ TWRWQLQEEA QRRRHTLYAK
PGQQEQLREE EELQREKRRQ EREREYREEE KLQREEDEKR RRQERERQYR ELEELRQEEQ
LRDRKLREEE QLLQEREEER LRRQERERKL REEEQLLRQE EQELRQERER KLREEEQLLR
REEQELRQER ERKLREEEQL LQEREEERLR RQERARKLRE EEQLLRQEEQ ELRQERERKL
REEEQLLRRE EQLLRQERDR KLREEEQLLQ ESEEERLRRQ EREQQLRRER DRKFREEEQL
LQEREEERLR RQERERKLRE EEQLLQEREE ERLRRQERER KLREEEQLLQ EREEERLRRQ
ERERKLREEE QLLRQEEQEL RQERARKLRE EEQLLRQEEQ ELRQERDRKL REEEQLLRQE
EQELRQERDR KLREEEQLLQ ESEEERLRRQ ERERKLREEE QLLRREEQEL RRERARKLRE
EEQLLQEREE ERLRRQERAR KLREEEQLLR REEQELRQER DRKFREEEQL LQEREEERLR
RQERDRKFRE EERQLRRQEL EEQFRQERDR KFRLEEQIRQ EKEEKQLRRQ ERDRKFREEE
QQRRRQEREQ QLRRERDRKF REEEQLLQER EEERLRRQER ARKLREEEQL LRREEQLLRQ
ERDRKFREEE QLLQESEEER LRRQERERKL REEEQLLQER EEERLRRQER ARKLREEEQL
LRQEEQELRQ ERARKLREEE QLLRQEEQEL RQERDRKFRE EEQLLRREEQ ELRRERDRKF
REEEQLLQER EEERLRRQER ARKLREEEEQ LLFEEQEEQR LRQERDRRYR AEEQFAREEK
SRRLERELRQ EEEQRRRRER ERKFREEQLR RQQEEEQRRR QLRERQFRED QSRRQVLEPG
TRQFARVPVR SSPLYEYIQE QRSQYRP
