TRHY_SHEEP
ID TRHY_SHEEP Reviewed; 1549 AA.
AC P22793;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Trichohyalin;
GN Name=TCHH; Synonyms=THH;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7684041; DOI=10.1083/jcb.121.4.855;
RA Fietz M.J., McLaughlan C.J., Campbell M.T., Rogers G.E.;
RT "Analysis of the sheep trichohyalin gene: potential structural and calcium-
RT binding roles of trichohyalin in the hair follicle.";
RL J. Cell Biol. 121:855-865(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1016-1549.
RC STRAIN=Merino-Dorset horn X Border Leicester; TISSUE=Wool follicle;
RX PubMed=2298812; DOI=10.1083/jcb.110.2.427;
RA Fietz M.J., Presland R.B., Rogers G.E.;
RT "The cDNA-deduced amino acid sequence for trichohyalin, a differentiation
RT marker in the hair follicle, contains a 23 amino acid repeat.";
RL J. Cell Biol. 110:427-436(1990).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=P22793-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P22793-2; Sequence=VSP_000847, VSP_000848;
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 epithelia of the tongue, hoof and rumen.
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}.
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DR EMBL; Z18361; CAA79165.1; -; Genomic_DNA.
DR EMBL; X51695; CAA35992.1; -; mRNA.
DR PIR; A40691; A40691.
DR AlphaFoldDB; P22793; -.
DR SMR; P22793; -.
DR STRING; 9940.ENSOARP00000022657; -.
DR PRIDE; P22793; -.
DR eggNOG; ENOG502QQH0; Eukaryota.
DR Proteomes; UP000002356; 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 Alternative splicing; Calcium; Citrullination; Keratinization;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..1549
FT /note="Trichohyalin"
FT /id="PRO_0000144044"
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 REPEAT 413..448
FT /note="1-1"
FT REPEAT 449..476
FT /note="1-2"
FT REPEAT 477..504
FT /note="1-3"
FT REPEAT 505..532
FT /note="1-4"
FT REPEAT 533..560
FT /note="1-5"
FT REPEAT 561..588
FT /note="1-6"
FT REPEAT 589..616
FT /note="1-7"
FT REPEAT 617..644
FT /note="1-8"
FT REPEAT 645..678
FT /note="1-9"
FT REPEAT 679..706
FT /note="1-10"
FT REPEAT 707..742
FT /note="1-11"
FT REPEAT 743..771
FT /note="1-12"
FT REPEAT 772..796
FT /note="1-13"
FT REPEAT 797..832
FT /note="1-14"
FT REPEAT 938..961
FT /note="2-1"
FT REPEAT 962..985
FT /note="2-2"
FT REPEAT 986..1021
FT /note="2-3"
FT REPEAT 1022..1044
FT /note="2-4"
FT REPEAT 1045..1067
FT /note="2-5"
FT REPEAT 1068..1090
FT /note="2-6"
FT REPEAT 1091..1121
FT /note="2-7"
FT REPEAT 1122..1144
FT /note="2-8"
FT REPEAT 1145..1167
FT /note="2-9"
FT REPEAT 1168..1197
FT /note="2-10"
FT REPEAT 1198..1227
FT /note="2-11"
FT REPEAT 1228..1250
FT /note="2-12"
FT REPEAT 1251..1273
FT /note="2-13"
FT REPEAT 1274..1296
FT /note="2-14"
FT REPEAT 1297..1319
FT /note="2-15"
FT REPEAT 1320..1342
FT /note="2-16"
FT REPEAT 1343..1368
FT /note="2-17"
FT REPEAT 1369..1391
FT /note="2-18"
FT REPEAT 1392..1416
FT /note="2-19"
FT REPEAT 1417..1439
FT /note="2-20"
FT REPEAT 1440..1461
FT /note="2-21"
FT REPEAT 1462..1484
FT /note="2-22"
FT REPEAT 1485..1507
FT /note="2-23"
FT REGION 1..91
FT /note="S-100-like"
FT REGION 97..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..832
FT /note="14 X 28 AA approximate tandem repeats"
FT REGION 782..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1507
FT /note="23 X 23 AA approximate tandem repeats"
FT REGION 980..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1520
FT /note="Basic and acidic 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 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 VAR_SEQ 1145..1197
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_000847"
FT VAR_SEQ 1251..1273
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_000848"
FT CONFLICT 1399
FT /note="E -> G (in Ref. 2; CAA35992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1549 AA; 201173 MW; E72FB9FF1326E54E CRC64;
MSPLLRSIFN ITKIFNQYAS HDCDGTTLSK KDLKNLLERE FGEILRKPHD PETVDLVLEL
QDRDRDGLID FHEFLAIVFK VAAACYYALG QASGLNEKEA KCERKGNPLQ DRRREDQRRF
EPQDRQLEER RLKRQELEEL AEEEELREKQ VRREQRLQRR EQEEYGGEEE LQQRPKGREL
EELLNREQRF ERQEQRERQR LQVEQQQRQR GELRERQEEV QLQKRETQEL QRERLEEEQQ
LQKQKRGLEE RLLEQERREQ ELRRKEQERR EQQLRQEQEE ATQEEISERG ESRTSRCQWQ
LESEADARQR KVYSRPHRQE QQSRRQEQEL LERQQEQQIS EEVQSLQEDQ GRQRLKQEQR
YDQNWRWQLE EESQRRRYTL YAKPAQREQV REEEQLRLKE EKLQREKRRQ ERERQYREVE
LQREEERLQR EEEQLQREER EKRRRQEREK QYLEKVELWE EEQLQREERE KRRQEREKQY
LEKVELREEE QLQRQEREKR RQERERQYLE KVELQEEEQL QREEREKRRQ ERERQYLEKV
ELQEEEQLQR QEREKRRQER EKQYLEKVEL QEEEQLQRQE RQKRRQEREK QYLEKVELQE
EEQLQRQERE KRRQERERQY LEKVELQEEE QVQRQEREKR RQERERQYLE KELQRQEERL
QEEEQLLREE REKRRQERER QYLEKVELQE EEQLQREERE KRRQERERQY LEKEELQRQE
ERLQREKEQL QREDREKRRQ VRERKYLEEE LQQEEDRLQR EKQLLREDRE KRQYLEKVEL
QREEEQLQRE KRRQERERQY REEELLREEE RLHRKEQQLQ REECEKRRRQ ELERQLEEEE
LQRLDRKRQF RDDDQHQNEV RNSRVYSKHR ENKEKSRQLD DSWVRESQFQ QDLRPLQDEQ
EEKREREQEW RSRQKRDSQF PAEQLLEREQ QKETERRDRK FREEEQLLKG QREEKIRYLE
EDRKFREEEQ QLRRLEREQQ LRQERDRKFR EELSRQERDR KFREEEQLLQ EREEQLRRQE
RDRKFREEEQ LLQEREEQLR RQERDRKFRE EEQLLQEREE QLRRQERDRK FREEEQQLRL
LEREQQLRQE RNRKFREEQL LREREEQLRL QEGEPQLRQK RDRKFHEEEQ LLQEREEQLR
RQERDRKFRE EAQILKEREE QLRRQERDRK FREEEQLLQE REELRRQERE PQLRQERDRK
FREEEQLLQE REKLRRQERE PQLRQERDRK FHEEEQLLQE REEQLRRQER DRKFREEAQL
LQEREEQLRR QERDRKFREE EQLLQEREEQ LRRQERDRKF REEEQLLQER EEQLRRQERD
RKFREEEQLL KESEEQLRRQ ERDRKFHEKE HLLREREEQQ LRRQELEGVF SQEEQLRRAE
QEEEQRRQRQ RDRKFLEEEQ SLQREREEEK RRVQEQDRKF LEQEEQLHRE EQEELRRRQQ
LDQQYRAEEQ FAREEKRRRQ EQELRQEEQR RRQERERKFR EEEQLRRQQQ EEQKRRQERD
VQQSRRQVWE EDKGRRQVLE AGKRQFASAP VRSSPLYEYI QEQRSQYRP
