PRM1A_DANRE
ID PRM1A_DANRE Reviewed; 826 AA.
AC Q9W735; B3DJD7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Prominin-1-A;
DE AltName: Full=Prominin-like protein 1;
GN Name=prom1a; Synonyms=proml1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-713.
RC TISSUE=Liver;
RX PubMed=12514187; DOI=10.1074/jbc.m210640200;
RA Fargeas C.A., Florek M., Huttner W.B., Corbeil D.;
RT "Characterization of prominin-2, a new member of the prominin family of
RT pentaspan membrane glycoproteins.";
RL J. Biol. Chem. 278:8586-8596(2003).
CC -!- FUNCTION: May play a role in cell differentiation, proliferation and
CC apoptosis. Binds cholesterol in cholesterol-containing plasma membrane
CC microdomains and may play a role in the organization of the apical
CC plasma membrane in epithelial cells. Involved in regulation of MAPK and
CC Akt signaling pathways (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell projection, microvillus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prominin family. {ECO:0000305}.
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DR EMBL; BC163446; AAI63446.1; -; mRNA.
DR EMBL; AF160970; AAD44341.1; -; mRNA.
DR RefSeq; NP_001108615.2; NM_001115143.2.
DR AlphaFoldDB; Q9W735; -.
DR SMR; Q9W735; -.
DR STRING; 7955.ENSDARP00000096190; -.
DR PaxDb; Q9W735; -.
DR PRIDE; Q9W735; -.
DR GeneID; 322857; -.
DR KEGG; dre:322857; -.
DR CTD; 322857; -.
DR ZFIN; ZDB-GENE-030131-1577; prom1a.
DR eggNOG; KOG4331; Eukaryota.
DR InParanoid; Q9W735; -.
DR OrthoDB; 1129032at2759; -.
DR PhylomeDB; Q9W735; -.
DR PRO; PR:Q9W735; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0071914; C:prominosome; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR InterPro; IPR008795; Prominin.
DR PANTHER; PTHR22730; PTHR22730; 1.
DR Pfam; PF05478; Prominin; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..826
FT /note="Prominin-1-A"
FT /id="PRO_0000218280"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 122
FT /note="V -> I (in Ref. 2; AAD44341)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..153
FT /note="LRGL -> FEDF (in Ref. 2; AAD44341)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="F -> L (in Ref. 2; AAD44341)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="T -> A (in Ref. 2; AAD44341)"
FT /evidence="ECO:0000305"
FT CONFLICT 613..614
FT /note="VN -> LS (in Ref. 2; AAD44341)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="N -> T (in Ref. 2; AAD44341)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="S -> T (in Ref. 2; AAD44341)"
FT /evidence="ECO:0000305"
FT CONFLICT 711..712
FT /note="ED -> GR (in Ref. 2; AAD44341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 826 AA; 91947 MW; 9AFD3BBDBAF25AD7 CRC64;
MLWKTALIFL CWGLTSGELQ NGLSATPAAP ARRTLDFGFV PSGVYDTVAY YEPGAIGILF
NMMHAFLFVV QPNPFPEDLV ISAAKDKFGA IQSEYQKVIY YELGFVVCAA LGLLFTVLLP
LVGLLFCLCR CCDNCGGEMH QRQRKNADCL RGLLTTLLLT TTFIITAGVL CAYAANQNLS
SQLKGMRRLV KSNLKDLHTF ANQTPAQIDY LISRYGTVKE QVLHDLENVG VILGGRIHEE
LGKEVKPALD ATLSMTGTMR DTKDALENVS LTLETLQEGT VKLQANLSVV RNSLRNALND
PVCVDAPAPE ICRNIRNSIP KLEIAANYSS LPDVTDQLNK VNDVLKTDLS QIVAKGIASF
NDTPAMVTAQ TRNIVEGVKV LLDDIGNNIT SFSKMLPVHS SLANFTRMIS HTHSQIEDIY
PQIDQMDFYR WIGCITLCCM IVLILTFNFL GLLCGILGFD RHASPTTRGC VSNTGGNFLM
AGVGFSFLFS WVLMGVITAL FLAGGNLEKL VCEPFQTRQL FKVLDTPYLV NSAWRNFIPG
YLYNDPEMDL TAYSLYSNCK DNRGIYSALH LDRIFNISSF FNTSVYSKDV SRKFEGLKVD
LRGIILLESE GKVNLNNFSE TGINEIDFAA YLEEVNKGVT RIDLIDFANQ LDAQADQLSK
GTLQTSLKGH ANTIRQIHIQ QVVPLEQSMS TLNQSIRLLE RTSSDLPLRV EDVLKAVDDA
QNLISYNATF VINQETEKYK QNIIGYFKQY IDWIRTSLAL EVATCKPLSN IVDTVEILGC
GFLLDSMNTF WFGLGCCTLF LLPSIILSVK LAKFYRRMDT EDVYDE
