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COLE_LEPMA
ID   COLE_LEPMA              Reviewed;         419 AA.
AC   P98085; Q91080;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-JUN-2021, entry version 82.
DE   RecName: Full=Inner ear-specific collagen;
DE   AltName: Full=Saccular collagen;
DE   Flags: Precursor;
OS   Lepomis macrochirus (Bluegill) (Eupomotis macrochirus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Centrarchiformes; Centrarchoidei; Centrarchidae; Lepomis.
OX   NCBI_TaxID=13106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7863331; DOI=10.1126/science.7863331;
RA   Davis J.G., Oberholtzer J.C., Burns F.R., Greene M.I.;
RT   "Molecular cloning and characterization of an inner ear-specific structural
RT   protein.";
RL   Science 267:1031-1034(1995).
CC   -!- FUNCTION: Forms a microstructural matrix within the otolithic membrane.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Specialized secretory supporting cells at the outer
CC       perimeter of the saccular epithelium.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69978.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U17431; AAA69978.1; ALT_FRAME; mRNA.
DR   PIR; A55797; A55797.
DR   PRIDE; P98085; -.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 4.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; SSF49842; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   2: Evidence at transcript level;
KW   Collagen; Extracellular matrix; Glycoprotein; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..419
FT                   /note="Inner ear-specific collagen"
FT                   /id="PRO_0000005712"
FT   DOMAIN          275..412
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          20..57
FT                   /note="Nonhelical region (NC2)"
FT   REGION          58..274
FT                   /note="Triple-helical region (COL1)"
FT   REGION          61..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..419
FT                   /note="Nonhelical region (NC1)"
FT   COMPBIAS        133..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   419 AA;  43635 MW;  570CDB9675FC0F39 CRC64;
     MDAYSLSPTD STTYSSDTFS TEFHTDAIAP PGNTPGNYTL DYNECFFNFC ECCPPEKGPM
     GPMGERGLPG PPGERGPLGL PGEKGETGLR GPPGPAGLPG ANGLNGDIGE KGDQGPVGLP
     GVPGIPGKPG EKGDPGLKGD KGERGFSGLK GDPGERGEPG LNGTKGSIGR EGPMGPGLAG
     TKGLKGEQGL KGECLQGEKG ERGPPGLRGE MGLNGTDGVK GERGEPGPLG GKGDTGARGP
     PGPPGGRGMA GLRGEKGLKG VRGPRGPKGP PGESVEQIRS AFSVGLFPSR SFPPPSLPVK
     FDKVFYNGEG HWDPTLNKFN VTYPGVYLFS YHITVRNRPV RAALVVNGVR KLRTRDSLYG
     QDIDQASNLA LLHLTDGDQV WLETLRDWNG XYSSSEDDST FSGFLLYPDT KKPTAMENL
 
 
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