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NPT2B_HUMAN
ID   NPT2B_HUMAN             Reviewed;         690 AA.
AC   O95436; A5PL17; Q8N2K2; Q8WYA9; Q9P0V7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 3.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Sodium-dependent phosphate transport protein 2B;
DE            Short=Sodium-phosphate transport protein 2B;
DE   AltName: Full=Na(+)-dependent phosphate cotransporter 2B;
DE   AltName: Full=NaPi3b;
DE   AltName: Full=Sodium/phosphate cotransporter 2B;
DE            Short=Na(+)/Pi cotransporter 2B;
DE            Short=NaPi-2b;
DE   AltName: Full=Solute carrier family 34 member 2;
GN   Name=SLC34A2;
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] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES
RP   (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION (ISOFORM 1), TRANSPORTER ACTIVITY
RP   (ISOFORM 1), AND VARIANT GLY-634.
RC   TISSUE=Lung, and Small intestine;
RX   PubMed=10329428; DOI=10.1006/bbrc.1999.0666;
RA   Feild J.A., Zhang L., Brun K.A., Brooks D.P., Edwards R.M.;
RT   "Cloning and functional characterization of a sodium-dependent phosphate
RT   transporter expressed in human lung and small intestine.";
RL   Biochem. Biophys. Res. Commun. 258:578-582(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), TRANSPORTER
RP   ACTIVITY (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT GLY-634.
RC   TISSUE=Small intestine;
RX   PubMed=10610722; DOI=10.1006/geno.1999.6009;
RA   Xu H., Bai L., Collins J.F., Ghishan F.K.;
RT   "Molecular cloning, functional characterization, tissue distribution, and
RT   chromosomal localization of a human, small intestinal sodium-phosphate
RT   (Na+-Pi) transporter (SLC34A2).";
RL   Genomics 62:281-284(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-634.
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-592 (ISOFORM 2), AND INDUCTION.
RC   TISSUE=Intestine;
RX   PubMed=11171583; DOI=10.1152/ajpcell.2001.280.3.c628;
RA   Xu H., Collins J.F., Bai L., Kiela P.R., Ghishan F.K.;
RT   "Regulation of the human sodium-phosphate cotransporter NaPi-IIb gene
RT   promoter by epidermal growth factor.";
RL   Am. J. Physiol. 280:C628-C636(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 266-690, AND VARIANT GLY-634.
RC   TISSUE=Ovarian carcinoma;
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   [7]
RP   DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH ROS1.
RX   PubMed=12661006; DOI=10.1002/gcc.10207;
RA   Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H.,
RA   Housman D.;
RT   "Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma with
RT   an interstitial del(6)(q21q21).";
RL   Genes Chromosomes Cancer 37:58-71(2003).
RN   [8]
RP   VARIANT PULAM ARG-106.
RX   PubMed=16960801; DOI=10.1086/508263;
RA   Corut A., Senyigit A., Ugur S.A., Altin S., Ozcelik U., Calisir H.,
RA   Yildirim Z., Gocmen A., Tolun A.;
RT   "Mutations in SLC34A2 cause pulmonary alveolar microlithiasis and are
RT   possibly associated with testicular microlithiasis.";
RL   Am. J. Hum. Genet. 79:650-656(2006).
CC   -!- FUNCTION: Involved in actively transporting phosphate into cells via
CC       Na(+) cotransport. {ECO:0000269|PubMed:10329428}.
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC         Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000269|PubMed:10329428};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256;
CC         Evidence={ECO:0000305|PubMed:10329428};
CC   -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC       Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC         Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000269|PubMed:10610722};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256;
CC         Evidence={ECO:0000305|PubMed:10610722};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC       pH dependence:
CC         Optimum pH is 6.6. {ECO:0000269|PubMed:10329428};
CC   -!- INTERACTION:
CC       O95436-2; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-12811757, EBI-11957045;
CC       O95436-2; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12811757, EBI-711490;
CC       O95436-2; Q02747: GUCA2A; NbExp=3; IntAct=EBI-12811757, EBI-12244272;
CC       O95436-2; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-12811757, EBI-10266796;
CC       O95436-2; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12811757, EBI-2820517;
CC       O95436-2; P26678: PLN; NbExp=3; IntAct=EBI-12811757, EBI-692836;
CC       O95436-2; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-12811757, EBI-8652812;
CC       O95436-2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-12811757, EBI-10244780;
CC       O95436-2; Q99726: SLC30A3; NbExp=5; IntAct=EBI-12811757, EBI-10294651;
CC       O95436-2; P78382: SLC35A1; NbExp=3; IntAct=EBI-12811757, EBI-12870360;
CC       O95436-2; Q92504: SLC39A7; NbExp=3; IntAct=EBI-12811757, EBI-1051105;
CC       O95436-2; P0DN84: STRIT1; NbExp=3; IntAct=EBI-12811757, EBI-12200293;
CC       O95436-2; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-12811757, EBI-10329860;
CC       O95436-2; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-12811757, EBI-10694905;
CC       O95436-2; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-12811757, EBI-11528917;
CC       O95436-2; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-12811757, EBI-12038591;
CC       O95436-2; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-12811757, EBI-12195249;
CC       O95436-2; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-12811757, EBI-11988865;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q9DBP0}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localized at the brush border membranes of
CC       enterocytes. {ECO:0000250|UniProtKB:Q9DBP0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=NaPi-3b;
CC         IsoId=O95436-1; Sequence=Displayed;
CC       Name=2; Synonyms=NaPi-2b, NaPi-IIb;
CC         IsoId=O95436-2; Sequence=VSP_016755;
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung. Also detected in
CC       pancreas, kidney, small intestine, ovary, testis, prostate and mammary
CC       gland. In lung, it is found in alveolar type II cells but not in
CC       bronchiolar epithelium. {ECO:0000269|PubMed:10329428,
CC       ECO:0000269|PubMed:10610722}.
CC   -!- INDUCTION: Down-regulated by EGF. {ECO:0000269|PubMed:11171583}.
CC   -!- DISEASE: Pulmonary alveolar microlithiasis (PULAM) [MIM:265100]: Rare
CC       disease characterized by the deposition of calcium phosphate microliths
CC       throughout the lungs. Most patients are asymptomatic for several years
CC       or even for decades and generally, the diagnosis is incidental to
CC       clinical investigations unrelated to the disease. Cases with early-
CC       onset or rapid progression are rare. A 'sandstorm-appearing' chest
CC       roentgenogram is a typical diagnostic finding. The onset of this
CC       potentially lethal disease varies from the neonatal period to old age
CC       and the disease follows a long-term, progressive course, resulting in a
CC       slow deterioration of lung functions. Pulmonary alveolar microlithiasis
CC       is a recessive monogenic disease with full penetrance.
CC       {ECO:0000269|PubMed:16960801}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Note=A chromosomal aberration involving SLC34A2 is found in a
CC       glioblastoma multiforme cell line U-118MG. Results in the formation of
CC       a SLC34A2-ROS1 chimeric protein that retains a constitutive kinase
CC       activity. {ECO:0000269|PubMed:12661006}.
CC   -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC11354.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF111856; AAC98695.1; -; mRNA.
DR   EMBL; AF146796; AAF31328.1; -; mRNA.
DR   EMBL; AC092436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC142704; AAI42705.1; -; mRNA.
DR   EMBL; BC146666; AAI46667.1; -; mRNA.
DR   EMBL; AH011306; AAL55657.1; -; Genomic_DNA.
DR   EMBL; AK075015; BAC11354.1; ALT_INIT; mRNA.
DR   CCDS; CCDS3435.1; -. [O95436-1]
DR   CCDS; CCDS54750.1; -. [O95436-2]
DR   RefSeq; NP_001171469.1; NM_001177998.1. [O95436-2]
DR   RefSeq; NP_001171470.1; NM_001177999.1. [O95436-2]
DR   RefSeq; NP_006415.2; NM_006424.2. [O95436-1]
DR   AlphaFoldDB; O95436; -.
DR   BioGRID; 115819; 50.
DR   IntAct; O95436; 33.
DR   STRING; 9606.ENSP00000371483; -.
DR   ChEMBL; CHEMBL4295685; -.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   DrugBank; DB14502; Sodium phosphate, dibasic.
DR   DrugBank; DB09449; Sodium phosphate, monobasic.
DR   DrugBank; DB14503; Sodium phosphate, monobasic, unspecified form.
DR   TCDB; 2.A.58.1.4; the phosphate:na(+) symporter (pnas) family.
DR   GlyGen; O95436; 5 sites.
DR   iPTMnet; O95436; -.
DR   PhosphoSitePlus; O95436; -.
DR   BioMuta; SLC34A2; -.
DR   MassIVE; O95436; -.
DR   MaxQB; O95436; -.
DR   PaxDb; O95436; -.
DR   PeptideAtlas; O95436; -.
DR   PRIDE; O95436; -.
DR   ProteomicsDB; 50879; -. [O95436-1]
DR   ProteomicsDB; 50880; -. [O95436-2]
DR   ABCD; O95436; 1 sequenced antibody.
DR   Antibodypedia; 51936; 155 antibodies from 25 providers.
DR   DNASU; 10568; -.
DR   Ensembl; ENST00000382051.8; ENSP00000371483.3; ENSG00000157765.13. [O95436-1]
DR   Ensembl; ENST00000503434.5; ENSP00000423021.1; ENSG00000157765.13. [O95436-2]
DR   Ensembl; ENST00000504570.5; ENSP00000425501.1; ENSG00000157765.13. [O95436-2]
DR   Ensembl; ENST00000645788.1; ENSP00000494094.1; ENSG00000157765.13. [O95436-2]
DR   GeneID; 10568; -.
DR   KEGG; hsa:10568; -.
DR   MANE-Select; ENST00000382051.8; ENSP00000371483.3; NM_006424.3; NP_006415.3.
DR   UCSC; uc003grr.4; human. [O95436-1]
DR   CTD; 10568; -.
DR   DisGeNET; 10568; -.
DR   GeneCards; SLC34A2; -.
DR   HGNC; HGNC:11020; SLC34A2.
DR   HPA; ENSG00000157765; Tissue enriched (lung).
DR   MalaCards; SLC34A2; -.
DR   MIM; 265100; phenotype.
DR   MIM; 604217; gene.
DR   neXtProt; NX_O95436; -.
DR   OpenTargets; ENSG00000157765; -.
DR   Orphanet; 60025; Pulmonary alveolar microlithiasis.
DR   PharmGKB; PA35888; -.
DR   VEuPathDB; HostDB:ENSG00000157765; -.
DR   eggNOG; ENOG502QQ3I; Eukaryota.
DR   GeneTree; ENSGT00950000183177; -.
DR   HOGENOM; CLU_025063_0_0_1; -.
DR   InParanoid; O95436; -.
DR   OMA; GCPKCCR; -.
DR   OrthoDB; 976094at2759; -.
DR   PhylomeDB; O95436; -.
DR   TreeFam; TF313981; -.
DR   BioCyc; MetaCyc:ENSG00000157765-MON; -.
DR   PathwayCommons; O95436; -.
DR   Reactome; R-HSA-427589; Type II Na+/Pi cotransporters.
DR   Reactome; R-HSA-5619045; Defective SLC34A2 causes pulmonary alveolar microlithiasis (PALM).
DR   Reactome; R-HSA-5683826; Surfactant metabolism.
DR   Reactome; R-HSA-5687583; Defective SLC34A2 causes PALM.
DR   SignaLink; O95436; -.
DR   SIGNOR; O95436; -.
DR   BioGRID-ORCS; 10568; 13 hits in 1067 CRISPR screens.
DR   ChiTaRS; SLC34A2; human.
DR   GeneWiki; SLC34A2; -.
DR   GenomeRNAi; 10568; -.
DR   Pharos; O95436; Tchem.
DR   PRO; PR:O95436; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; O95436; protein.
DR   Bgee; ENSG00000157765; Expressed in lower lobe of lung and 109 other tissues.
DR   ExpressionAtlas; O95436; baseline and differential.
DR   Genevisible; O95436; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005903; C:brush border; IBA:GO_Central.
DR   GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR   GO; GO:0042301; F:phosphate ion binding; IDA:UniProtKB.
DR   GO; GO:0031402; F:sodium ion binding; IDA:UniProtKB.
DR   GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR   GO; GO:0030643; P:cellular phosphate ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0006817; P:phosphate ion transport; IDA:UniProtKB.
DR   GO; GO:0043627; P:response to estrogen; IEP:UniProtKB.
DR   GO; GO:0044341; P:sodium-dependent phosphate transport; IBA:GO_Central.
DR   InterPro; IPR003841; Na/Pi_transpt.
DR   InterPro; IPR029852; Na/Pi_transpt_2B.
DR   PANTHER; PTHR10010; PTHR10010; 1.
DR   PANTHER; PTHR10010:SF23; PTHR10010:SF23; 1.
DR   Pfam; PF02690; Na_Pi_cotrans; 2.
DR   TIGRFAMs; TIGR01013; 2a58; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW   Glycoprotein; Ion transport; Membrane; Reference proteome; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..690
FT                   /note="Sodium-dependent phosphate transport protein 2B"
FT                   /id="PRO_0000068613"
FT   TOPO_DOM        1..100
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        122..135
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..212
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical; Name=M3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical; Name=M4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..407
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical; Name=M5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..485
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..506
FT                   /note="Helical; Name=M6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..525
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        526..546
FT                   /note="Helical; Name=M7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        547..552
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        553..573
FT                   /note="Helical; Name=M8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        574..689
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            126..127
FT                   /note="Breakpoint for translocation to form a SLC34A2-ROS1
FT                   fusion protein"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        303..350
FT                   /evidence="ECO:0000250|UniProtKB:Q06496"
FT   VAR_SEQ         38..39
FT                   /note="TD -> N (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10610722,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016755"
FT   VARIANT         45
FT                   /note="V -> A (in dbSNP:rs35426730)"
FT                   /id="VAR_034156"
FT   VARIANT         106
FT                   /note="G -> R (in PULAM; dbSNP:rs137853142)"
FT                   /evidence="ECO:0000269|PubMed:16960801"
FT                   /id="VAR_030677"
FT   VARIANT         634
FT                   /note="D -> G (in dbSNP:rs6448389)"
FT                   /evidence="ECO:0000269|PubMed:10329428,
FT                   ECO:0000269|PubMed:10610722, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_030678"
FT   CONFLICT        228
FT                   /note="V -> L (in Ref. 2; AAF31328 and 5; AAL55657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="T -> V (in Ref. 6; BAC11354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590..595
FT                   /note="Missing (in Ref. 6; BAC11354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        620
FT                   /note="C -> Y (in Ref. 1; AAC98695)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   690 AA;  75759 MW;  3BDB1920CA92C035 CRC64;
     MAPWPELGDA QPNPDKYLEG AAGQQPTAPD KSKETNKTDN TEAPVTKIEL LPSYSTATLI
     DEPTEVDDPW NLPTLQDSGI KWSERDTKGK ILCFFQGIGR LILLLGFLYF FVCSLDILSS
     AFQLVGGKMA GQFFSNSSIM SNPLLGLVIG VLVTVLVQSS STSTSIVVSM VSSSLLTVRA
     AIPIIMGANI GTSITNTIVA LMQVGDRSEF RRAFAGATVH DFFNWLSVLV LLPVEVATHY
     LEIITQLIVE SFHFKNGEDA PDLLKVITKP FTKLIVQLDK KVISQIAMND EKAKNKSLVK
     IWCKTFTNKT QINVTVPSTA NCTSPSLCWT DGIQNWTMKN VTYKENIAKC QHIFVNFHLP
     DLAVGTILLI LSLLVLCGCL IMIVKILGSV LKGQVATVIK KTINTDFPFP FAWLTGYLAI
     LVGAGMTFIV QSSSVFTSAL TPLIGIGVIT IERAYPLTLG SNIGTTTTAI LAALASPGNA
     LRSSLQIALC HFFFNISGIL LWYPIPFTRL PIRMAKGLGN ISAKYRWFAV FYLIIFFFLI
     PLTVFGLSLA GWRVLVGVGV PVVFIIILVL CLRLLQSRCP RVLPKKLQNW NFLPLWMRSL
     KPWDAVVSKF TGCFQMRCCC CCRVCCRACC LLCDCPKCCR CSKCCEDLEE AQEGQDVPVK
     APETFDNITI SREAQGEVPA SDSKTECTAL
 
 
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