S35F2_HUMAN
ID S35F2_HUMAN Reviewed; 374 AA.
AC Q8IXU6; Q14963; Q5JPA8; Q6ZRQ3; Q9H947;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Solute carrier family 35 member F2;
GN Name=SLC35F2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Lymph;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-261 (ISOFORMS 1/2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-164 (ISOFORM 3).
RX PubMed=9119394; DOI=10.1006/geno.1996.4595;
RA Stankovic T., Byrd P.J., Cooper P.R., McConville C.M., Munroe D.J.,
RA Riley J.H., Watts G.D.J., Ambrose H., McGuire G., Smith A.D., Sutcliffe A.,
RA Mills T., Taylor A.M.R.;
RT "Construction of a transcription map around the gene for ataxia
RT telangiectasia; identification of at least four novel genes.";
RL Genomics 40:267-276(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Putative solute transporter. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IXU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IXU6-2; Sequence=VSP_028700, VSP_028701;
CC Name=3;
CC IsoId=Q8IXU6-3; Sequence=VSP_028699;
CC -!- SIMILARITY: Belongs to the SLC35F solute transporter family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68226.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK023080; BAB14394.1; -; mRNA.
DR EMBL; AK128062; BAC87256.1; -; mRNA.
DR EMBL; BC039195; AAH39195.1; -; mRNA.
DR EMBL; BC048302; AAH48302.1; -; mRNA.
DR EMBL; AL833969; CAI46204.1; -; Transcribed_RNA.
DR EMBL; X99961; CAA68226.1; ALT_INIT; mRNA.
DR CCDS; CCDS41709.1; -. [Q8IXU6-1]
DR RefSeq; NP_059985.2; NM_017515.4. [Q8IXU6-1]
DR AlphaFoldDB; Q8IXU6; -.
DR SMR; Q8IXU6; -.
DR BioGRID; 120116; 79.
DR IntAct; Q8IXU6; 12.
DR STRING; 9606.ENSP00000436785; -.
DR TCDB; 2.A.7.24.10; the drug/metabolite transporter (dmt) superfamily.
DR iPTMnet; Q8IXU6; -.
DR PhosphoSitePlus; Q8IXU6; -.
DR BioMuta; SLC35F2; -.
DR DMDM; 74728243; -.
DR EPD; Q8IXU6; -.
DR jPOST; Q8IXU6; -.
DR MassIVE; Q8IXU6; -.
DR MaxQB; Q8IXU6; -.
DR PaxDb; Q8IXU6; -.
DR PeptideAtlas; Q8IXU6; -.
DR PRIDE; Q8IXU6; -.
DR ProteomicsDB; 71065; -. [Q8IXU6-1]
DR ProteomicsDB; 71066; -. [Q8IXU6-2]
DR ProteomicsDB; 71067; -. [Q8IXU6-3]
DR Antibodypedia; 31913; 70 antibodies from 19 providers.
DR DNASU; 54733; -.
DR Ensembl; ENST00000375682.8; ENSP00000364834.4; ENSG00000110660.15. [Q8IXU6-3]
DR Ensembl; ENST00000525071.5; ENSP00000434307.1; ENSG00000110660.15. [Q8IXU6-2]
DR Ensembl; ENST00000525815.6; ENSP00000436785.1; ENSG00000110660.15. [Q8IXU6-1]
DR GeneID; 54733; -.
DR KEGG; hsa:54733; -.
DR MANE-Select; ENST00000525815.6; ENSP00000436785.1; NM_017515.5; NP_059985.2.
DR UCSC; uc001pjq.3; human. [Q8IXU6-1]
DR CTD; 54733; -.
DR DisGeNET; 54733; -.
DR GeneCards; SLC35F2; -.
DR HGNC; HGNC:23615; SLC35F2.
DR HPA; ENSG00000110660; Tissue enhanced (salivary).
DR neXtProt; NX_Q8IXU6; -.
DR OpenTargets; ENSG00000110660; -.
DR PharmGKB; PA134945023; -.
DR VEuPathDB; HostDB:ENSG00000110660; -.
DR eggNOG; KOG2766; Eukaryota.
DR GeneTree; ENSGT00390000015655; -.
DR HOGENOM; CLU_039639_0_0_1; -.
DR InParanoid; Q8IXU6; -.
DR OMA; LRVRYHW; -.
DR OrthoDB; 659967at2759; -.
DR PhylomeDB; Q8IXU6; -.
DR TreeFam; TF313645; -.
DR PathwayCommons; Q8IXU6; -.
DR SignaLink; Q8IXU6; -.
DR BioGRID-ORCS; 54733; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; SLC35F2; human.
DR GenomeRNAi; 54733; -.
DR Pharos; Q8IXU6; Tbio.
DR PRO; PR:Q8IXU6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8IXU6; protein.
DR Bgee; ENSG00000110660; Expressed in cortical plate and 152 other tissues.
DR ExpressionAtlas; Q8IXU6; baseline and differential.
DR Genevisible; Q8IXU6; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR009262; SLC35_F1/F2/F6.
DR Pfam; PF06027; SLC35F; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..374
FT /note="Solute carrier family 35 member F2"
FT /id="PRO_0000307309"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TML3"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9119394"
FT /id="VSP_028699"
FT VAR_SEQ 314..358
FT /note="FSGLYILSFTVIMVGFILYCSTPTRTAEPAESSVPPVTSIGIDNL -> DST
FT SCPSLSSWWGLSCTAPPLLARPSRLKAACLQSPALGLTTW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028700"
FT VAR_SEQ 360..374
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028701"
FT CONFLICT 48
FT /note="M -> T (in Ref. 1; BAB14394)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="T -> A (in Ref. 4; CAA68226)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="S -> SG (in Ref. 3; CAI46204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 41212 MW; ADBF0F42F2DC7998 CRC64;
MEADSPAGPG APEPLAEGAA AEFSSLLRRI KGKLFTWNIL KTIALGQMLS LCICGTAITS
QYLAERYKVN TPMLQSFINY CLLFLIYTVM LAFRSGSDNL LVILKRKWWK YILLGLADVE
ANYVIVRAYQ YTTLTSVQLL DCFGIPVLMA LSWFILHARY RVIHFIAVAV CLLGVGTMVG
ADILAGREDN SGSDVLIGDI LVLLGASLYA ISNVCEEYIV KKLSRQEFLG MVGLFGTIIS
GIQLLIVEYK DIASIHWDWK IALLFVAFAL CMFCLYSFMP LVIKVTSATS VNLGILTADL
YSLFVGLFLF GYKFSGLYIL SFTVIMVGFI LYCSTPTRTA EPAESSVPPV TSIGIDNLGL
KLEENLQETH SAVL
