SPNS1_HUMAN
ID SPNS1_HUMAN Reviewed; 528 AA.
AC Q9H2V7; B5MDM9; Q6P182; Q71RB5; Q7L541; Q86VU7; Q8N953; Q8TCS5; Q9BRN5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein spinster homolog 1;
DE AltName: Full=HSpin1;
DE AltName: Full=Spinster-like protein 1;
GN Name=SPNS1; Synonyms=SPIN1; ORFNames=PP20300;
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).
RX PubMed=11340170; DOI=10.1128/mcb.21.11.3775-3788.2001;
RA Nakano Y., Fujitani K., Kurihara J., Ragan J., Usui-Aoki K., Shimoda L.,
RA Lukacsovich T., Suzuki K., Sezaki M., Sano Y., Ueda R., Awano W.,
RA Kaneda M., Umeda M., Yamamoto D.;
RT "Mutations in the novel membrane protein spinster interfere with programmed
RT cell death and cause neural degeneration in Drosophila melanogaster.";
RL Mol. Cell. Biol. 21:3775-3788(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary cancer;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP PRO-230.
RC TISSUE=Blood, Brain, Pancreas, and Skin;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BCL2 AND BCL2L1.
RX PubMed=12815463; DOI=10.1038/sj.cdd.4401246;
RA Yanagisawa H., Miyashita T., Nakano Y., Yamamoto D.;
RT "HSpin1, a transmembrane protein interacting with Bcl-2/Bcl-xL, induces a
RT caspase-independent autophagic cell death.";
RL Cell Death Differ. 10:798-807(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, 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).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Sphingolipid transporter (By similarity). May be involved in
CC necrotic or autophagic cell death. {ECO:0000250,
CC ECO:0000269|PubMed:12815463}.
CC -!- SUBUNIT: Interacts with BCL2 and BCL2L1. {ECO:0000269|PubMed:12815463}.
CC -!- INTERACTION:
CC Q9H2V7; Q07817: BCL2L1; NbExp=3; IntAct=EBI-1386527, EBI-78035;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12815463}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12815463}. Note=Colocalizes with SDHB.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H2V7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2V7-2; Sequence=VSP_028196;
CC Name=3; Synonyms=CRA_d;
CC IsoId=Q9H2V7-3; Sequence=VSP_028195, VSP_028196;
CC Name=4;
CC IsoId=Q9H2V7-4; Sequence=VSP_028194;
CC Name=5;
CC IsoId=Q9H2V7-5; Sequence=VSP_036389;
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster (TC
CC 2.A.1.49) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ15259.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ15259.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF212371; AAG43830.1; -; mRNA.
DR EMBL; AK095677; BAC04603.1; -; mRNA.
DR EMBL; AK289787; BAF82476.1; -; mRNA.
DR EMBL; AF370423; AAQ15259.1; ALT_SEQ; mRNA.
DR EMBL; AL390215; CAB99229.1; -; mRNA.
DR EMBL; AC109460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471267; EAW52018.1; -; Genomic_DNA.
DR EMBL; CH471267; EAW52019.1; -; Genomic_DNA.
DR EMBL; BC006156; AAH06156.1; -; mRNA.
DR EMBL; BC008325; AAH08325.1; -; mRNA.
DR EMBL; BC038961; AAH38961.1; -; mRNA.
DR EMBL; BC047741; AAH47741.1; -; mRNA.
DR EMBL; BC065235; AAH65235.1; -; mRNA.
DR CCDS; CCDS10646.1; -. [Q9H2V7-1]
DR CCDS; CCDS45452.1; -. [Q9H2V7-2]
DR CCDS; CCDS45453.1; -. [Q9H2V7-3]
DR CCDS; CCDS45454.1; -. [Q9H2V7-4]
DR RefSeq; NP_001135920.1; NM_001142448.1. [Q9H2V7-1]
DR RefSeq; NP_001135921.1; NM_001142449.1. [Q9H2V7-3]
DR RefSeq; NP_001135922.1; NM_001142450.1. [Q9H2V7-4]
DR RefSeq; NP_001135923.1; NM_001142451.1. [Q9H2V7-2]
DR RefSeq; NP_114427.1; NM_032038.2. [Q9H2V7-1]
DR AlphaFoldDB; Q9H2V7; -.
DR SMR; Q9H2V7; -.
DR BioGRID; 123836; 106.
DR IntAct; Q9H2V7; 31.
DR MINT; Q9H2V7; -.
DR STRING; 9606.ENSP00000309945; -.
DR TCDB; 2.A.1.49.2; the major facilitator superfamily (mfs).
DR GlyGen; Q9H2V7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H2V7; -.
DR PhosphoSitePlus; Q9H2V7; -.
DR BioMuta; SPNS1; -.
DR DMDM; 74733566; -.
DR EPD; Q9H2V7; -.
DR jPOST; Q9H2V7; -.
DR MassIVE; Q9H2V7; -.
DR MaxQB; Q9H2V7; -.
DR PaxDb; Q9H2V7; -.
DR PeptideAtlas; Q9H2V7; -.
DR PRIDE; Q9H2V7; -.
DR ProteomicsDB; 80600; -. [Q9H2V7-1]
DR ProteomicsDB; 80601; -. [Q9H2V7-2]
DR ProteomicsDB; 80602; -. [Q9H2V7-3]
DR ProteomicsDB; 80604; -. [Q9H2V7-5]
DR Antibodypedia; 26665; 80 antibodies from 20 providers.
DR DNASU; 83985; -.
DR Ensembl; ENST00000311008.16; ENSP00000309945.11; ENSG00000169682.18. [Q9H2V7-1]
DR Ensembl; ENST00000323081.12; ENSP00000318228.8; ENSG00000169682.18. [Q9H2V7-4]
DR Ensembl; ENST00000334536.12; ENSP00000335494.8; ENSG00000169682.18. [Q9H2V7-2]
DR Ensembl; ENST00000352260.11; ENSP00000306050.10; ENSG00000169682.18. [Q9H2V7-3]
DR GeneID; 83985; -.
DR KEGG; hsa:83985; -.
DR MANE-Select; ENST00000311008.16; ENSP00000309945.11; NM_032038.3; NP_114427.1.
DR UCSC; uc002drx.3; human. [Q9H2V7-1]
DR CTD; 83985; -.
DR DisGeNET; 83985; -.
DR GeneCards; SPNS1; -.
DR HGNC; HGNC:30621; SPNS1.
DR HPA; ENSG00000169682; Low tissue specificity.
DR MIM; 612583; gene.
DR neXtProt; NX_Q9H2V7; -.
DR OpenTargets; ENSG00000169682; -.
DR PharmGKB; PA162404561; -.
DR VEuPathDB; HostDB:ENSG00000169682; -.
DR eggNOG; KOG1330; Eukaryota.
DR GeneTree; ENSGT00390000005976; -.
DR HOGENOM; CLU_001265_5_12_1; -.
DR InParanoid; Q9H2V7; -.
DR OMA; DQMVMSP; -.
DR OrthoDB; 891881at2759; -.
DR PhylomeDB; Q9H2V7; -.
DR TreeFam; TF314395; -.
DR PathwayCommons; Q9H2V7; -.
DR SignaLink; Q9H2V7; -.
DR BioGRID-ORCS; 83985; 80 hits in 1085 CRISPR screens.
DR ChiTaRS; SPNS1; human.
DR GenomeRNAi; 83985; -.
DR Pharos; Q9H2V7; Tbio.
DR PRO; PR:Q9H2V7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H2V7; protein.
DR Bgee; ENSG00000169682; Expressed in granulocyte and 96 other tissues.
DR ExpressionAtlas; Q9H2V7; baseline and differential.
DR Genevisible; Q9H2V7; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd17328; MFS_spinster_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR044770; MFS_spinster-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR23505; PTHR23505; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Lipid transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..528
FT /note="Protein spinster homolog 1"
FT /id="PRO_0000305039"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_028194"
FT VAR_SEQ 81..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028195"
FT VAR_SEQ 223..528
FT /note="TPGLGVVAVLLLFLVVREPPRGAVERHSDLPPLNPTSWWADLRALARNPSFV
FT LSSLGFTAVAFVTGSLALWAPAFLLRSRVVLGETPPCLPGDSCSSSDSLIFGLITCLTG
FT VLGVGLGVEISRRLRHSNPRADPLVCATGLLGSAPFLFLSLACARGSIVATYIFIFIGE
FT TLLSMNWAIVADILLYVVIPTRRSTAEAFQIVLSHLLGDAGSPYLIGLISDRLRRNWPP
FT SFLSEFRALQFSLMLCAFVGALGGAAFLGTAIFIEADRRRAQLHVQGLLHEAGSTDDRI
FT VVPQRGRSTRVPVASVLI -> SLVLAWG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036389"
FT VAR_SEQ 271..322
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_028196"
FT VARIANT 230
FT /note="A -> P (in dbSNP:rs17855956)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035157"
SQ SEQUENCE 528 AA; 56630 MW; F1B9D2EB3F9F1B48 CRC64;
MAGSDTAPFL SQADDPDDGP VPGTPGLPGS TGNPKSEEPE VPDQEGLQRI TGLSPGRSAL
IVAVLCYINL LNYMDRFTVA GVLPDIEQFF NIGDSSSGLI QTVFISSYMV LAPVFGYLGD
RYNRKYLMCG GIAFWSLVTL GSSFIPGEHF WLLLLTRGLV GVGEASYSTI APTLIADLFV
ADQRSRMLSI FYFAIPVGSG LGYIAGSKVK DMAGDWHWAL RVTPGLGVVA VLLLFLVVRE
PPRGAVERHS DLPPLNPTSW WADLRALARN PSFVLSSLGF TAVAFVTGSL ALWAPAFLLR
SRVVLGETPP CLPGDSCSSS DSLIFGLITC LTGVLGVGLG VEISRRLRHS NPRADPLVCA
TGLLGSAPFL FLSLACARGS IVATYIFIFI GETLLSMNWA IVADILLYVV IPTRRSTAEA
FQIVLSHLLG DAGSPYLIGL ISDRLRRNWP PSFLSEFRAL QFSLMLCAFV GALGGAAFLG
TAIFIEADRR RAQLHVQGLL HEAGSTDDRI VVPQRGRSTR VPVASVLI
