K2C73_HUMAN
ID K2C73_HUMAN Reviewed; 540 AA.
AC Q86Y46; Q32MB2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Keratin, type II cytoskeletal 73;
DE AltName: Full=Cytokeratin-73;
DE Short=CK-73;
DE AltName: Full=Keratin-73;
DE Short=K73;
DE AltName: Full=Type II inner root sheath-specific keratin-K6irs3;
DE AltName: Full=Type-II keratin Kb36;
GN Name=KRT73; Synonyms=K6IRS3, KB36, KRT6IRS3;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Scalp;
RX PubMed=12648212; DOI=10.1046/j.1523-1747.2003.12087.x;
RA Langbein L., Rogers M.A., Praetzel S., Winter H., Schweizer J.;
RT "K6irs1, K6irs2, K6irs3, and K6irs4 represent the inner-root-sheath-
RT specific type II epithelial keratins of the human hair follicle.";
RL J. Invest. Dermatol. 120:512-522(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16874310; DOI=10.1038/sj.jid.5700494;
RA Langbein L., Rogers M.A., Praetzel-Wunder S., Helmke B., Schirmacher P.,
RA Schweizer J.;
RT "K25 (K25irs1), K26 (K25irs2), K27 (K25irs3), and K28 (K25irs4) represent
RT the type I inner root sheath keratins of the human hair follicle.";
RL J. Invest. Dermatol. 126:2377-2386(2006).
RN [5]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-212 AND MET-248.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Has a role in hair formation. Specific component of keratin
CC intermediate filaments in the inner root sheath (IRS) of the hair
CC follicle (Probable). {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC -!- INTERACTION:
CC Q86Y46; P19012: KRT15; NbExp=3; IntAct=EBI-2830994, EBI-739566;
CC Q86Y46-2; P19012: KRT15; NbExp=3; IntAct=EBI-12039441, EBI-739566;
CC Q86Y46-2; P08779: KRT16; NbExp=3; IntAct=EBI-12039441, EBI-356410;
CC Q86Y46-2; Q15323: KRT31; NbExp=3; IntAct=EBI-12039441, EBI-948001;
CC Q86Y46-2; O76013-2: KRT36; NbExp=3; IntAct=EBI-12039441, EBI-11958506;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86Y46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86Y46-2; Sequence=VSP_030417, VSP_030418;
CC -!- TISSUE SPECIFICITY: Highly expressed in hair follicles from scalp. In
CC hair, it is specifically present in the inner root sheath (IRS) of the
CC hair follicle. Present in the IRS cuticle, but not in Henle or Huxley
CC layers of the IRS. In the IRS cuticle, it is expressed between the
CC lowermost bulb region of the cuticle and the region where Henle cells
CC undergo abrupt terminal differentiation. Detected up to the uppermost
CC cortex region where cuticle cells terminally differentiate (at protein
CC level). {ECO:0000269|PubMed:12648212, ECO:0000269|PubMed:16874310}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC respectively).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AJ508776; CAD48513.1; -; mRNA.
DR EMBL; CH471054; EAW96640.1; -; Genomic_DNA.
DR EMBL; BC109212; AAI09213.1; -; mRNA.
DR EMBL; BC109213; AAI09214.1; -; mRNA.
DR CCDS; CCDS8834.1; -. [Q86Y46-1]
DR RefSeq; NP_778238.1; NM_175068.2. [Q86Y46-1]
DR AlphaFoldDB; Q86Y46; -.
DR SMR; Q86Y46; -.
DR BioGRID; 130489; 42.
DR IntAct; Q86Y46; 16.
DR MINT; Q86Y46; -.
DR STRING; 9606.ENSP00000307014; -.
DR iPTMnet; Q86Y46; -.
DR PhosphoSitePlus; Q86Y46; -.
DR SwissPalm; Q86Y46; -.
DR BioMuta; KRT73; -.
DR DMDM; 74750553; -.
DR jPOST; Q86Y46; -.
DR MassIVE; Q86Y46; -.
DR PaxDb; Q86Y46; -.
DR PeptideAtlas; Q86Y46; -.
DR PRIDE; Q86Y46; -.
DR ProteomicsDB; 70373; -. [Q86Y46-1]
DR ProteomicsDB; 70374; -. [Q86Y46-2]
DR Antibodypedia; 51267; 112 antibodies from 17 providers.
DR DNASU; 319101; -.
DR Ensembl; ENST00000305748.7; ENSP00000307014.3; ENSG00000186049.8. [Q86Y46-1]
DR GeneID; 319101; -.
DR KEGG; hsa:319101; -.
DR MANE-Select; ENST00000305748.7; ENSP00000307014.3; NM_175068.3; NP_778238.1.
DR UCSC; uc001sas.3; human. [Q86Y46-1]
DR CTD; 319101; -.
DR DisGeNET; 319101; -.
DR GeneCards; KRT73; -.
DR HGNC; HGNC:28928; KRT73.
DR HPA; ENSG00000186049; Tissue enriched (skin).
DR MIM; 608247; gene.
DR neXtProt; NX_Q86Y46; -.
DR OpenTargets; ENSG00000186049; -.
DR PharmGKB; PA147031702; -.
DR VEuPathDB; HostDB:ENSG00000186049; -.
DR eggNOG; ENOG502SK67; Eukaryota.
DR GeneTree; ENSGT00940000161853; -.
DR HOGENOM; CLU_012560_6_1_1; -.
DR InParanoid; Q86Y46; -.
DR OMA; ARMMCEY; -.
DR OrthoDB; 671547at2759; -.
DR PhylomeDB; Q86Y46; -.
DR TreeFam; TF317854; -.
DR PathwayCommons; Q86Y46; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q86Y46; -.
DR BioGRID-ORCS; 319101; 10 hits in 1062 CRISPR screens.
DR GenomeRNAi; 319101; -.
DR Pharos; Q86Y46; Tdark.
DR PRO; PR:Q86Y46; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86Y46; protein.
DR Bgee; ENSG00000186049; Expressed in skin of leg and 61 other tissues.
DR ExpressionAtlas; Q86Y46; baseline and differential.
DR Genevisible; Q86Y46; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Intermediate filament; Keratin;
KW Reference proteome.
FT CHAIN 1..540
FT /note="Keratin, type II cytoskeletal 73"
FT /id="PRO_0000314881"
FT DOMAIN 132..445
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..131
FT /note="Head"
FT REGION 132..167
FT /note="Coil 1A"
FT REGION 168..186
FT /note="Linker 1"
FT REGION 187..278
FT /note="Coil 1B"
FT REGION 279..302
FT /note="Linker 12"
FT REGION 303..441
FT /note="Coil 2"
FT REGION 442..540
FT /note="Tail"
FT REGION 502..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 383
FT /note="Stutter"
FT VAR_SEQ 371..381
FT /note="CANLETAIADA -> VKGTGAFLTHS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030417"
FT VAR_SEQ 382..540
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030418"
FT VARIANT 61
FT /note="V -> M (in dbSNP:rs35417182)"
FT /id="VAR_038091"
FT VARIANT 96
FT /note="P -> L (in dbSNP:rs659436)"
FT /id="VAR_038092"
FT VARIANT 212
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1210935768)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038093"
FT VARIANT 248
FT /note="T -> M (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs142246988)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038094"
FT VARIANT 365
FT /note="E -> G (in dbSNP:rs607426)"
FT /id="VAR_038095"
FT CONFLICT 11
FT /note="A -> P (in Ref. 3; AAI09214/AAI09213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 58923 MW; 7B4FC058FDE3191B CRC64;
MSRQFTYKSG AAAKGGFSGC SAVLSGGSSS SYRAGGKGLS GGFSSRSLYS LGGARSISFN
VASGSGWAGG YGFGRGRASG FAGSMFGSVA LGSVCPSLCP PGGIHQVTIN KSLLAPLNVE
LDPEIQKVRA QEREQIKVLN NKFASFIDKV RFLEQQNQVL ETKWELLQQL DLNNCKNNLE
PILEGYISNL RKQLETLSGD RVRLDSELRS VREVVEDYKK RYEEEINKRT TAENEFVVLK
KDVDAAYTSK VELQAKVDAL DGEIKFFKCL YEGETAQIQS HISDTSIILS MDNNRNLDLD
SIIAEVRAQY EEIARKSKAE AEALYQTKFQ ELQLAAGRHG DDLKHTKNEI SELTRLIQRL
RSEIESVKKQ CANLETAIAD AEQRGDCALK DARAKLDELE GALQQAKEEL ARMLREYQEL
LSVKLSLDIE IATYRKLLEG EECRMSGEYT NSVSISVINS SMAGMAGTGA GFGFSNAGTY
GYWPSSVSGG YSMLPGGCVT GSGNCSPRGE ARTRLGSASE FRDSQGKTLA LSSPTKKTMR
