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SFTPA_CANLF
ID   SFTPA_CANLF             Reviewed;         248 AA.
AC   P06908;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Pulmonary surfactant-associated protein A;
DE            Short=PSAP;
DE            Short=PSP-A;
DE            Short=SP-A;
DE   Flags: Precursor;
GN   Name=SFTPA1; Synonyms=SFTP1, SFTPA;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SIGNAL SEQUENCE CLEAVAGE SITE.
RX   PubMed=3863100; DOI=10.1073/pnas.82.19.6379;
RA   Benson B., Hawgood S., Schilling J., Clements J., Damm D., Cordell B.,
RA   White R.T.;
RT   "Structure of canine pulmonary surfactant apoprotein: cDNA and complete
RT   amino acid sequence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6379-6383(1985).
RN   [2]
RP   DOMAIN.
RX   PubMed=3808053; DOI=10.1038/325490a0;
RA   Patthy L.;
RT   "Is lung surfactant protein a lectin-collagen hybrid?";
RL   Nature 325:490-490(1987).
CC   -!- FUNCTION: In presence of calcium ions, it binds to surfactant
CC       phospholipids and contributes to lower the surface tension at the air-
CC       liquid interface in the alveoli of the mammalian lung and is essential
CC       for normal respiration. Enhances the expression of MYO18A/SP-R210 on
CC       alveolar macrophages. {ECO:0000250|UniProtKB:P35242}.
CC   -!- SUBUNIT: Oligomeric complex of 6 set of homotrimers.
CC       {ECO:0000250|UniProtKB:Q8IWL2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8IWL2}.
CC       Secreted, extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:Q8IWL2}. Secreted, extracellular space, surface
CC       film {ECO:0000250|UniProtKB:Q8IWL2}.
CC   -!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10%
CC       protein. There are 4 surfactant-associated proteins: 2 collagenous,
CC       carbohydrate-binding glycoproteins (SP-A and SP-D) and 2 small
CC       hydrophobic proteins (SP-B and SP-C).
CC   -!- SIMILARITY: Belongs to the SFTPA family. {ECO:0000305}.
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DR   EMBL; M11769; AAA30887.1; -; mRNA.
DR   PIR; A25296; LNDGPS.
DR   AlphaFoldDB; P06908; -.
DR   SMR; P06908; -.
DR   STRING; 9615.ENSCAFP00000023171; -.
DR   PaxDb; P06908; -.
DR   InParanoid; P06908; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR   CDD; cd03591; CLECT_collectin_like; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR033990; Collectin_CTLD.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Collagen; Disulfide bond; Extracellular matrix; Gaseous exchange;
KW   Glycoprotein; Hydroxylation; Lectin; Metal-binding; Reference proteome;
KW   Repeat; Secreted; Signal; Surface film.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:3863100"
FT   CHAIN           18..248
FT                   /note="Pulmonary surfactant-associated protein A"
FT                   /id="PRO_0000017454"
FT   DOMAIN          28..100
FT                   /note="Collagen-like"
FT   DOMAIN          132..248
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          29..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         215
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         30
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         33
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         36
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         54
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         57
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         63
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         67
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         70
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        155..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        224..238
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   248 AA;  26269 MW;  340FE95D4E2502C0 CRC64;
     MWLRCLALAL TLLMVSGIEN NTKDVCVGNP GIPGTPGSHG LPGRDGRDGV KGDPGPPGPL
     GPPGGMPGHP GPNGMTGAPG VAGERGEKGE PGERGPPGLP ASLDEELQTT LHDLRHQILQ
     TMGVLSLHES LLVVGRKVFS SNAQSINFND IQELCAGAGG QIAAPMSPEE NEAVASIVKK
     YNTYAYLGLV ESPDSGDFQY MDGAPVNYTN WYPGEPRGRG KEQCVEMYTD GQWNNKNCLQ
     YRLAICEF
 
 
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