ID   TMM79_BOVIN             Reviewed;         395 AA.
AC   Q5E9U3; A4FV77;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Transmembrane protein 79;
DE   AltName: Full=Mattrin;
GN   Name=TMEM79;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Contributes to the epidermal integrity and skin barrier
CC       function. Plays a role in the lamellar granule (LG) secretory system
CC       and in the stratum corneum (SC) epithelial cell formation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. Golgi apparatus, trans-
CC       Golgi network {ECO:0000250}. Membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}. Note=Colocalized with TGOLN2 in the
CC       trans-Golgi network. Colocalized with LAMP1 in the lysosome (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; BT020827; AAX08844.1; -; mRNA.
DR   EMBL; BC123830; AAI23831.1; -; mRNA.
DR   RefSeq; NP_001014920.1; NM_001014920.1.
DR   AlphaFoldDB; Q5E9U3; -.
DR   STRING; 9913.ENSBTAP00000012416; -.
DR   PaxDb; Q5E9U3; -.
DR   Ensembl; ENSBTAT00000012416; ENSBTAP00000012416; ENSBTAG00000009436.
DR   GeneID; 513599; -.
DR   KEGG; bta:513599; -.
DR   CTD; 84283; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009436; -.
DR   VGNC; VGNC:36112; TMEM79.
DR   eggNOG; ENOG502QVUB; Eukaryota.
DR   GeneTree; ENSGT00390000002390; -.
DR   HOGENOM; CLU_062246_1_0_1; -.
DR   InParanoid; Q5E9U3; -.
DR   OMA; YYMFLVE; -.
DR   OrthoDB; 963760at2759; -.
DR   TreeFam; TF333310; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000009436; Expressed in digestive system secreted substance and 101 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0070268; P:cornification; IEA:Ensembl.
DR   GO; GO:0042335; P:cuticle development; IEA:Ensembl.
DR   GO; GO:0002070; P:epithelial cell maturation; ISS:UniProtKB.
DR   GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR   GO; GO:0045684; P:positive regulation of epidermis development; ISS:UniProtKB.
DR   GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Lysosome; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..395
FT                   /note="Transmembrane protein 79"
FT                   /id="PRO_0000254117"
FT   TOPO_DOM        1..204
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..244
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..290
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        312..313
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..395
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..101
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  43502 MW;  0216D118850A6B3A CRC64;
     MTEPETLALL EVKGPETLEK SPPQALVPNG RKLEGEDEVE SLGAESSRVG SSAESPTARE
     GTEDGLDSTV SEAATLPWGT GPQPSAPFPD PPGWRNIEPE PPESEPPTKL EELPEDEASL
     LPEKAARAFV PIDLQCIERR PQEDLVVCCE ASEGEHRRTF LPPRATHPEP PECKWAEAVV
     KPPGHSCGGC GGCGGREALR AVASVGAALI LFPCLLYGAY AFLPFDAPRL PTMSSRLIYT
     LRCGVFATFP IVLGILVYGL SLLCFAALRP FGEPRREVEI HRQYVAQSVQ LFILYFFNLA
     VLSTYLPQDA LKLLPLLTGL FAISRLIYWL TFAVGRSFRG FGYGLTFLPL LSMLLWNFYY
     MFVVEPERML TASESRLDYP DHARSASDYR PRSRG