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CCHCR_PANTR
ID   CCHCR_PANTR             Reviewed;         782 AA.
AC   Q8HZ60; Q7YR47;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Coiled-coil alpha-helical rod protein 1;
DE   AltName: Full=Alpha-helical coiled-coil rod protein;
GN   Name=CCHCR1; Synonyms=HCR;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Asumalahti K., Kere J.;
RT   "HCR gene orthologs in chimpanzee, pygmy chimpanzee, gorilla, and
RT   orangutan.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA   Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA   Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA   Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA   Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT   "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT   insertions/deletions as the major path to genomic divergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
CC   -!- FUNCTION: May be a regulator of keratinocyte proliferation or
CC       differentiation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC78167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY135777; AAN12279.1; -; Genomic_DNA.
DR   EMBL; AY135761; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135762; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135763; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135764; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135765; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135766; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135767; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135768; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135769; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135770; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135771; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135772; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135773; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135774; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135775; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; AY135776; AAN12279.1; JOINED; Genomic_DNA.
DR   EMBL; BA000041; BAC78167.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8HZ60; -.
DR   SMR; Q8HZ60; -.
DR   InParanoid; Q8HZ60; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central.
DR   InterPro; IPR009800; HCR.
DR   PANTHER; PTHR46822; PTHR46822; 1.
DR   Pfam; PF07111; HCR; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Developmental protein; Differentiation; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..782
FT                   /note="Coiled-coil alpha-helical rod protein 1"
FT                   /id="PRO_0000089419"
FT   REGION          62..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          82..314
FT                   /evidence="ECO:0000255"
FT   COILED          344..437
FT                   /evidence="ECO:0000255"
FT   COILED          498..691
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        62..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        288
FT                   /note="Q -> H (in Ref. 2; BAC78167)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="S -> T (in Ref. 2; BAC78167)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        638
FT                   /note="R -> H (in Ref. 2; BAC78167)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        671
FT                   /note="R -> Q (in Ref. 2; BAC78167)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   782 AA;  88660 MW;  D140F8587129D054 CRC64;
     MFPPSGSTGL IPPSHFQARP LSTLPRMAPT WLSDIPLVQP PGHQDVSERR LDTQRPQVTM
     WERDVSSDRQ EPGRRGRSWG LEGSQALSQQ AEVIARQLQE LRRLEEEVRL LRETSLQQKM
     RLEAQAMELE ALARAEKAGR AEAEGLRAAL AGAEVVRKNL EEGSQRELEE VQRLHQEQLS
     SLTQAHEEAL SSLTSKAEGL EKSLSSLETR RAGEAKELAE AQREAELLRK QLSKTQEDLE
     AQVTLVENLR KYVGEQVPSE VHSQTWELER QKLLETMQHL QEDRDSLQAT VELLQVRVQS
     LTHILALQEE ELTRKVQPSD SLEPEFTRKC QSLLNRWREK VFALMVQLKA QELEHSDSVK
     QLKGQVASLQ EKVTSQSQEQ AILQRSLQDK AAEVEVERMG AKGLQLELSR AQEARRRWQQ
     QTASAEEQLR LVVNAVSSSQ IWLETTMAKV EEAAAQLPSL NNRLSYAVRK VHTIRGLIAR
     KLALAQLRQE SCPLPPPVAD VSLELQQLRE ERNRLDAELQ LSARLIQQEV GRAREQGEAE
     RQQLSKVAQQ LEQELQQTQE SLASLGLQLE VARQGQQEST EEAASLRQEL TQQQELYGQA
     LQEKVAEVET RLREQLSDTE RRLNEARREH AKAVVSLRQI QRRAAQEKER SQELRRLQEE
     ARKEEGQRLA RRLQELERDK NLMLATLQQE GLLSRYKQQR LLTVLPSLLD KKKSVVSSPR
     PPECSASAPI AAAVPTRESI KGSLSVLLDD LQGLSEAISK EEAVCQGDNL DRCSSSNPQM
     SS
 
 
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