SHRM2_HUMAN
ID SHRM2_HUMAN Reviewed; 1616 AA.
AC Q13796; B9EIQ7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protein Shroom2;
DE AltName: Full=Apical-like protein;
DE AltName: Full=Protein APXL;
GN Name=SHROOM2; Synonyms=APXL;
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].
RC TISSUE=Retina;
RX PubMed=7795590; DOI=10.1093/hmg/4.3.373;
RA Schiaffino V.M., Bassi M.T., Rugarli E.I., Renieri A., Galli L.,
RA Ballabio A.;
RT "Cloning of a human homologue of the Xenopus laevis APX gene from the
RT ocular albinism type 1 critical region.";
RL Hum. Mol. Genet. 4:373-382(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P., Schiaffino M.V.,
RA Smith P., Staub O., Hildebrand J.D., Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974; SER-1036 AND SER-1039,
RP AND 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-851 AND SER-1039,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-1245.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in endothelial cell morphology changes during
CC cell spreading. In the retinal pigment epithelium, may regulate the
CC biogenesis of melanosomes and promote their association with the apical
CC cell surface by inducing gamma-tubulin redistribution (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000250}.
CC -!- INTERACTION:
CC Q13796; P16333: NCK1; NbExp=2; IntAct=EBI-1644065, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}. Cell
CC junction, tight junction {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Associates with cortical F-actin. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Abundant in retina and melanoma; also in brain,
CC placenta, lung, kidney and pancreas.
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
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DR EMBL; X83543; CAA58534.1; -; mRNA.
DR EMBL; AC002365; AAC32592.1; -; Genomic_DNA.
DR EMBL; AC090481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140866; AAI40867.1; -; mRNA.
DR CCDS; CCDS14135.1; -.
DR PIR; I37183; I37183.
DR RefSeq; NP_001307592.1; NM_001320663.1.
DR RefSeq; NP_001307593.1; NM_001320664.1.
DR RefSeq; NP_001640.1; NM_001649.3.
DR PDB; 5F4Y; X-ray; 3.29 A; A/B=1427-1610.
DR PDB; 5F5P; X-ray; 3.57 A; A/B/G/H=1427-1610.
DR PDBsum; 5F4Y; -.
DR PDBsum; 5F5P; -.
DR AlphaFoldDB; Q13796; -.
DR SMR; Q13796; -.
DR BioGRID; 106853; 15.
DR IntAct; Q13796; 13.
DR STRING; 9606.ENSP00000370299; -.
DR iPTMnet; Q13796; -.
DR PhosphoSitePlus; Q13796; -.
DR BioMuta; SHROOM2; -.
DR DMDM; 2498147; -.
DR EPD; Q13796; -.
DR jPOST; Q13796; -.
DR MassIVE; Q13796; -.
DR MaxQB; Q13796; -.
DR PaxDb; Q13796; -.
DR PeptideAtlas; Q13796; -.
DR PRIDE; Q13796; -.
DR ProteomicsDB; 59687; -.
DR Antibodypedia; 23655; 176 antibodies from 26 providers.
DR DNASU; 357; -.
DR Ensembl; ENST00000380913.8; ENSP00000370299.3; ENSG00000146950.13.
DR GeneID; 357; -.
DR KEGG; hsa:357; -.
DR MANE-Select; ENST00000380913.8; ENSP00000370299.3; NM_001649.4; NP_001640.1.
DR UCSC; uc004csu.2; human.
DR CTD; 357; -.
DR DisGeNET; 357; -.
DR GeneCards; SHROOM2; -.
DR HGNC; HGNC:630; SHROOM2.
DR HPA; ENSG00000146950; Tissue enhanced (retina).
DR MIM; 300103; gene.
DR neXtProt; NX_Q13796; -.
DR OpenTargets; ENSG00000146950; -.
DR PharmGKB; PA24916; -.
DR VEuPathDB; HostDB:ENSG00000146950; -.
DR eggNOG; ENOG502QUU2; Eukaryota.
DR GeneTree; ENSGT00940000155212; -.
DR HOGENOM; CLU_003220_0_0_1; -.
DR InParanoid; Q13796; -.
DR OMA; PFDAHVG; -.
DR OrthoDB; 29607at2759; -.
DR PhylomeDB; Q13796; -.
DR TreeFam; TF333370; -.
DR PathwayCommons; Q13796; -.
DR SignaLink; Q13796; -.
DR BioGRID-ORCS; 357; 18 hits in 702 CRISPR screens.
DR ChiTaRS; SHROOM2; human.
DR GenomeRNAi; 357; -.
DR Pharos; Q13796; Tbio.
DR PRO; PR:Q13796; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q13796; protein.
DR Bgee; ENSG00000146950; Expressed in middle temporal gyrus and 149 other tissues.
DR ExpressionAtlas; Q13796; baseline and differential.
DR Genevisible; Q13796; HS.
DR GO; GO:0005912; C:adherens junction; ISS:HGNC.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:HGNC.
DR GO; GO:0008013; F:beta-catenin binding; ISS:HGNC.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; TAS:ProtInc.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; ISS:HGNC-UCL.
DR GO; GO:0007420; P:brain development; ISS:HGNC-UCL.
DR GO; GO:0043010; P:camera-type eye development; ISS:HGNC-UCL.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0043482; P:cellular pigment accumulation; ISS:HGNC-UCL.
DR GO; GO:0043583; P:ear development; ISS:HGNC-UCL.
DR GO; GO:0032401; P:establishment of melanosome localization; ISS:HGNC-UCL.
DR GO; GO:0008057; P:eye pigment granule organization; ISS:HGNC-UCL.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISS:HGNC-UCL.
DR GO; GO:0032438; P:melanosome organization; ISS:HGNC-UCL.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR027686; Shroom2.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR PANTHER; PTHR15012:SF8; PTHR15012:SF8; 1.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; Developmental protein; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome; Tight junction.
FT CHAIN 1..1616
FT /note="Protein Shroom2"
FT /id="PRO_0000064650"
FT DOMAIN 26..108
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 684..773
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 1317..1611
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 128..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 925
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TP36"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TP36"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ALU4"
FT VARIANT 942
FT /note="D -> E (in dbSNP:rs16985780)"
FT /id="VAR_053896"
FT VARIANT 1245
FT /note="D -> H (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1033602309)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036577"
FT VARIANT 1475
FT /note="I -> V (in dbSNP:rs12012202)"
FT /id="VAR_053897"
FT VARIANT 1607
FT /note="L -> F (in dbSNP:rs2073942)"
FT /id="VAR_024250"
FT HELIX 1428..1436
FT /evidence="ECO:0007829|PDB:5F4Y"
FT HELIX 1438..1479
FT /evidence="ECO:0007829|PDB:5F4Y"
FT HELIX 1482..1519
FT /evidence="ECO:0007829|PDB:5F4Y"
FT HELIX 1527..1564
FT /evidence="ECO:0007829|PDB:5F4Y"
FT HELIX 1569..1604
FT /evidence="ECO:0007829|PDB:5F4Y"
SQ SEQUENCE 1616 AA; 176410 MW; 752406B5BC0B60A2 CRC64;
MEGAEPRARP ERLAEAETRA ADGGRLVEVQ LSGGAPWGFT LKGGREHGEP LVITKIEEGS
KAAAVDKLLA GDEIVGINDI GLSGFRQEAI CLVKGSHKTL KLVVKRRSEL GWRPHSWHAT
KFSDSHPELA ASPFTSTSGC PSWSGRHHAS SSSHDLSSSW EQTNLQRTLD HFSSLGSVDS
LDHPSSRLSV AKSNSSIDHL GSHSKRDSAY GSFSTSSSTP DHTLSKADTS SAENILYTVG
LWEAPRQGGR QAQAAGDPQG SEEKLSCFPP RVPGDSGKGP RPEYNAEPKL AAPGRSNFGP
VWYVPDKKKA PSSPPPPPPP LRSDSFAATK SHEKAQGPVF SEAAAAQHFT ALAQAQPRGD
RRPELTDRPW RSAHPGSLGK GSGGPGCPQE AHADGSWPPS KDGASSRLQA SLSSSDVRFP
QSPHSGRHPP LYSDHSPLCA DSLGQEPGAA SFQNDSPPQV RGLSSCDQKL GSGWQGPRPC
VQGDLQAAQL WAGCWPSDTA LGALESLPPP TVGQSPRHHL PQPEGPPDAR ETGRCYPLDK
GAEGCSAGAQ EPPRASRAEK ASQRLAASIT WADGESSRIC PQETPLLHSL TQEGKRRPES
SPEDSATRPP PFDAHVGKPT RRSDRFATTL RNEIQMHRAK LQKSRSTVAL TAAGEAEDGT
GRWRAGLGGG TQEGPLAGTY KDHLKEAQAR VLRATSFKRR DLDPNPGDLY PESLEHRMGD
PDTVPHFWEA GLAQPPSSTS GGPHPPRIGG RRRFTAEQKL KSYSEPEKMN EVGLTRGYSP
HQHPRTSEDT VGTFADRWKF FEETSKPVPQ RPAQKQALHG IPRDKPERPR TAGRTCEGTE
PWSRTTSLGD SLNAHSAAEK AGTSDLPRRL GTFAEYQASW KEQRKPLEAR SSGRCHSADD
ILDVSLDPQE RPQHVHGRSR SSPSTDHYKQ EASVELRRQA GDPGEPREEL PSAVRAEEGQ
STPRQADAQC REGSPGSQQH PPSQKAPNPP TFSELSHCRG APELPREGRG RAGTLPRDYR
YSEESTPADL GPRAQSPGSP LHARGQDSWP VSSALLSKRP APQRPPPPKR EPRRYRATDG
APADAPVGVL GRPFPTPSPA SLDVYVARLS LSHSPSVFSS AQPQDTPKAT VCERGSQHVS
GDASRPLPEA LLPPKQQHLR LQTATMETSR SPSPQFAPQK LTDKPPLLIQ DEDSTRIERV
MDNNTTVKMV PIKIVHSESQ PEKESRQSLA CPAEPPALPH GLEKDQIKTL STSEQFYSRF
CLYTRQGAEP EAPHRAQPAE PQPLGTQVPP EKDRCTSPPG LSYMKAKEKT VEDLKSEELA
REIVGKDKSL ADILDPSVKI KTTMDLMEGI FPKDEHLLEE AQQRRKLLPK IPSPRSTEER
KEEPSVPAAV SLATNSTYYS TSAPKAELLI KMKDLQEQQE HEEDSGSDLD HDLSVKKQEL
IESISRKLQV LREARESLLE DVQANTVLGA EVEAIVKGVC KPSEFDKFRM FIGDLDKVVN
LLLSLSGRLA RVENALNNLD DGASPGDRQS LLEKQRVLIQ QHEDAKELKE NLDRRERIVF
DILANYLSEE SLADYEHFVK MKSALIIEQR ELEDKIHLGE EQLKCLLDSL QPERGK
