SFTPA_RABIT
ID SFTPA_RABIT Reviewed; 247 AA.
AC P12842;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 138.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2830270; DOI=10.1016/s0021-9258(18)69159-8;
RA Boggaram V., Qing K., Mendelson C.R.;
RT "The major apoprotein of rabbit pulmonary surfactant. Elucidation of
RT primary sequence and cyclic AMP and developmental regulation.";
RL J. Biol. Chem. 263:2939-2947(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=1616051; DOI=10.1152/ajplung.1992.262.6.l662;
RA Chen Q., Boggaram V., Mendelson C.R.;
RT "Rabbit lung surfactant protein A gene: identification of a lung-specific
RT DNase I hypersensitive site.";
RL Am. J. Physiol. 262:L662-L671(1992).
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; J03542; AAA31465.1; -; mRNA.
DR EMBL; L19387; AAA31468.1; -; Genomic_DNA.
DR PIR; A29931; LNRBPS.
DR RefSeq; NP_001075698.1; NM_001082229.1.
DR RefSeq; XP_017206012.1; XM_017350523.1.
DR RefSeq; XP_017206013.1; XM_017350524.1.
DR AlphaFoldDB; P12842; -.
DR SMR; P12842; -.
DR STRING; 9986.ENSOCUP00000012830; -.
DR PRIDE; P12842; -.
DR GeneID; 100009044; -.
DR KEGG; ocu:100009044; -.
DR CTD; 653509; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P12842; -.
DR OrthoDB; 1172460at2759; -.
DR TreeFam; TF330481; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript 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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..247
FT /note="Pulmonary surfactant-associated protein A"
FT /id="PRO_0000017461"
FT DOMAIN 27..99
FT /note="Collagen-like"
FT DOMAIN 132..247
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 30..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 233
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 29
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 41
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 62
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 69
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 25
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 154..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 223..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 12
FT /note="S -> P"
FT CONFLICT 57..60
FT /note="GPMG -> APWA (in Ref. 2; AAA31468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 26071 MW; 289634054CBC8CB4 CRC64;
MLLLSLALTL ISAPASDTCD TKDVCIGSPG IPGTPGSHGL PGRDGRDGVK GDPGPPGPMG
PPGGMPGLPG RDGLIGAPGV PGERGDKGEP GERGPPGLPA YLDEELQATL HELRHHALQS
IGVLSLQGSM KAVGEKIFST NGQSVNFDAI REVCARAGGR IAVPRSLEEN EAIASIVKER
NTYAYLGLAE GPTAGDFYYL DGDPVNYTNW YPGEPRGQGR EKCVEMYTDG KWNDKNCLQY
RLVICEF
