ENK13_HUMAN
ID ENK13_HUMAN Reviewed; 482 AA.
AC Q9NX77; A8K9G3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Endogenous retrovirus group K member 13-1 Env polyprotein;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=HERV-K_16p13.3 provirus ancestral Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
GN Name=ERVK13-1;
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].
RA Isogai T., Sugiyama T., Otsuki T., Wakamatsu A., Sato H., Ishii S.,
RA Yamamoto J., Isono Y., Hio Y., Otsuka K., Nagai K., Irie R., Tamechika I.,
RA Seki N., Yoshikawa T., Otsuka M., Nagahari K., Masuho Y.;
RT "Full-length cDNA sequences.";
RL Patent number EP1308459, 07-MAY-2003.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ileal mucosa, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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).
CC -!- FUNCTION: Retroviral envelope proteins mediate receptor recognition and
CC membrane fusion during early infection. Endogenous envelope proteins
CC may have kept, lost or modified their original function during
CC evolution (By similarity). {ECO:0000250}.
CC -!- FUNCTION: SU mediates receptor recognition. {ECO:0000250}.
CC -!- FUNCTION: TM anchors the envelope heterodimer to the viral membrane
CC through one transmembrane domain. The other hydrophobic domain, called
CC fusion peptide, mediates fusion of the viral membrane with the target
CC cell membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The surface (SU) and transmembrane (TM) proteins form a
CC heterodimer. SU and TM are attached by noncovalent interactions or by a
CC labile interchain disulfide bond (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Primary culture of CD34+, lung, thymus, ileal
CC mucosa, small intestine, and testis.
CC -!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM
CC proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the beta type-B retroviral envelope protein
CC family. HERV class-II K(HML-4) env subfamily. {ECO:0000305}.
CC -!- CAUTION: No predictable signal peptide. {ECO:0000305}.
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DR EMBL; AX747190; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK000400; BAA91140.1; -; mRNA.
DR EMBL; AK091794; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK095440; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK097014; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK097909; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK292678; BAF85367.1; -; mRNA.
DR EMBL; BC043252; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q9NX77; -.
DR IntAct; Q9NX77; 1.
DR BioMuta; HGNC:27548; -.
DR DMDM; 47605749; -.
DR jPOST; Q9NX77; -.
DR PeptideAtlas; Q9NX77; -.
DR PRIDE; Q9NX77; -.
DR GeneCards; ERVK13-1; -.
DR HGNC; HGNC:27548; ERVK13-1.
DR neXtProt; NX_Q9NX77; -.
DR PhylomeDB; Q9NX77; -.
DR PathwayCommons; Q9NX77; -.
DR SignaLink; Q9NX77; -.
DR Pharos; Q9NX77; Tdark.
DR PRO; PR:Q9NX77; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9NX77; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR000328; GP41-like.
DR InterPro; IPR029104; HERV-K_env.
DR Pfam; PF00517; GP41; 1.
DR Pfam; PF13804; HERV-K_env_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond; ERV;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transposable element; Viral envelope protein; Virion.
FT CHAIN 1..482
FT /note="Endogenous retrovirus group K member 13-1 Env
FT polyprotein"
FT /id="PRO_0000008530"
FT CHAIN 1..289
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008531"
FT CHAIN 290..482
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008532"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 290..310
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT SITE 289..290
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="K -> E (in Ref. 1; AX747190 and 2; AK091794)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 55045 MW; A4AAD5B0E9B7AECC CRC64;
MWTVPSFTND SYQVYNVFST NSFQLLTVKR TPHEAWRVPL TTKTNKTKGL PDCPKKPTNG
PFIVTSILWD NCNAPKAVVL QTLAMGIVID WAPKGHYWQD CSSKNTLCSE FIYSLDYIEH
GWQSYTMRQR VSPYPFKWMD TGIAPPRPKI IHPFFTPEHP ELWKLAAALS GIKIWNTTYQ
LLRTKTKTPT FNITLISEWV IPIRSCVKPP YMLLVGNIIM MPDAQTIECH NCKLFTCIDA
TFNPTTSILL VRAREGVWIP VSLHRPWESS PSIHIVNEVL KDILKRTKRF IFTLIAVLAG
LLAVTATAAT AGVAIRSSVQ TAHYVEACQK NSSRLWNSQA QIDQKLANQI NDLRQSVTWL
GDRVMNLQHR MQLQCDWNTS DYCITPYAYN QDQHSWENVS RHLKAWDDNL TLDISQLKEQ
IFEASQAHLS TVPGSHIFEG ITKQLPDFNP FKWLKPVRGS LLLLALLILV CLCCLLLVCR
CL
