ID A0A493SW56_ANAPP Unreviewed; 859 AA.
AC A0A493SW56;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN Name=TMTC2 {ECO:0000313|Ensembl:ENSAPLP00000017728.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000017728.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000017728.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000017728.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TMTC family.
CC {ECO:0000256|ARBA:ARBA00007882}.
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DR AlphaFoldDB; A0A493SW56; -.
DR STRING; 8840.ENSAPLP00000017728; -.
DR Ensembl; ENSAPLT00000036706.1; ENSAPLP00000017728.1; ENSAPLG00000013866.2.
DR GeneTree; ENSGT00940000156144; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000016666; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44216; PROTEIN O-MANNOSYL-TRANSFERASE TMTC2; 1.
DR PANTHER; PTHR44216:SF3; PROTEIN O-MANNOSYL-TRANSFERASE TMTC2; 1.
DR Pfam; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13432; TPR_16; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..859
FT /note="dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019710651"
FT TRANSMEM 108..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 271..343
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
FT REPEAT 516..549
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 550..583
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 584..617
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 629..662
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 700..733
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 802..835
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 859 AA; 96780 MW; 5CF1F06A5B71D051 CRC64;
MFGPLSWLWL TAFLLTGCDL DLDVRTPWRL GRANKMGPIR SSRLTWAAEI SRAIKTNQDL
LPETPWTHIF YNDFWGTLLT HSGSHKSYRP LCTLSFRINH AVGGMDPWGY HLVNVLLHAA
VTGLFTNFSR ILFGDGYWTL IAGLLFASHP IHTEAVAGIV GRADIGACLF FLLSLMCYVK
HCSTRSSSAS TWGWILGTGV CAGCSMLWKE QGVTVLAISA VYDIFVFHRL KMHQIIPALY
KRKNLSLFFS IGLLTSWGTA LLGVRLYWMG NKPPSFSNSD NPAADSDSFL TRTLTFLYLP
TKNLWLLLCP DTLSFDWSMD AVPLLKAVSD WRNIHTVAFY AGLLLLAYFS LKGSGNEREC
NGRSVMNGKQ NANGHSCHSE VEYKTLEGKS SFASKEENGI KRHEIQKLQL PSTENIVILS
LSLLIVPFVP ATNLFFYVGF VIAERVLYVP SMGFCLLVTV GVRALYVKAQ KRFLKNLVFC
STAALIVFYG LKTVVRNGDW QNEEMLYRSG IKVNPAKAWG NLGNVLKSQS KISEAESAYR
NALYYRSNMA DMLYNLGLLL QENSRFSEAL HYYKLAIGSR PTLASAYLNT GIILMNQGKT
EEARKTFLKC SEISDENLKD PHAHKSSVTS CLYNLGKLFH EQGHYEDALT VYKEAIQKMP
RQFAPQSLYN MIGEAYMRMS RLPEAEHWYV ESLRSKSDHI PAHLTYGKLL ALTGRKSEAE
KYFVKAIQLD PTKGNCYMHY GQFLLEESRL IEAAEMAKKA AELDNTEFDV VFNAAHMLRQ
ASLNEEAEKY YEMAAGLRPN YPAALMNLGA ILHLNGKLKE AEENYLLALQ LKPDDVITQS
NLRKLWNIME KQGLKTAKT
//
