ID A0A2K5M8C8_CERAT Unreviewed; 1410 AA.
AC A0A2K5M8C8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=MIA SH3 domain ER export factor 2 {ECO:0000313|Ensembl:ENSCATP00000021466.1};
GN Name=MIA2 {ECO:0000313|Ensembl:ENSCATP00000021466.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000021466.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000021466.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR RefSeq; XP_011922581.1; XM_012067191.1.
DR STRING; 9531.ENSCATP00000021466; -.
DR Ensembl; ENSCATT00000045668.1; ENSCATP00000021466.1; ENSCATG00000034274.1.
DR GeneID; 105589100; -.
DR KEGG; caty:105589100; -.
DR CTD; 102689870; -.
DR GeneTree; ENSGT00950000182767; -.
DR OrthoDB; 5406966at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000034274; Expressed in adult mammalian kidney and 12 other cell types or tissues.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR CDD; cd11892; SH3_MIA2; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035555; MIA2_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23158:SF38; MELANOMA INHIBITORY ACTIVITY PROTEIN 2; 1.
DR PANTHER; PTHR23158; MELANOMA INHIBITORY ACTIVITY-RELATED; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014393985"
FT TRANSMEM 645..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..101
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 260..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 723..876
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 946..1093
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 269..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 160189 MW; 95058306A0FA944E CRC64;
MEKLGVHRIF LLAISLTKCL ESTKLLADLK KCGDLECETL ISRVSAMRDY RGPDCRYLNF
TKGEEISVFV KLAGEREDLW AGSKGKEFGY FPRDAVQIEE VFISEEIQMS TKESDFLCLL
GVSYTFDNED SELNSDYGEN IYPFEEDKDE KSSIYEGDFQ LEPGFYATYE STLFEDQFPA
LDAPEDVGST SESKNWEEAV VESVEQDHIP EVHVPPSSAV PGLKEWFGLR GEQAEEKAFE
SVIEPVQESS FRSRKIAVED ENDLEELNNG EPQTEHQQES ESEIDSVPKT HSELASESEH
VPKPQPTGWF GGGFTNYLGF GDEDTGLELL AEESNSPLQD FPNSISSDKE DTVPCTEILI
EKKDTITNDS LSLEPSWFDF GFAMLGFAYA KEDKIMLDDR KNEEDGGAGE HEYPLTNELD
PEKEQEIEMI QIMETEDQID KKPVLEKTDE SDAIPYLKKF LYNFDNPWNF QNTPKETELP
FPKQTLDQNN VIENEETEEF SIDNYPTDNT KVMMFESSYN PSDMVSNIEL PMRIHEEVHF
KPSSSKDSDE NSKPSVDTEG PALVEIDRSV ENTLLNNQMV STDNSLSSQN YISQKEDASE
FQILKYLFQI DGYDFMNSAF SSIVILTERV VAALPEGMRP DSYGFPWELV ICAALVGFFA
VIFFLWRSFR SVRSRLYVGR EKKLAVTLSG LIEEKCKLLE KFSLVQKEYE GYEVESSLKD
ASFEKEATEA QSLEATCEKL NRSKSELEDE IFCLEKELKE EKCKHSEQDE LMADISKRIQ
SLEDESKSLK SQVAEAKMTF RIFQMNEERL KIAIKDALNE NSQLQESEKQ LLQEAEVWKE
QVSELNKQKI TFEDSKVHAE QVLNDKENHI KTLTERLLKM KDWAAVLGED ITDDDNLELE
MNSESENGAY LDNPPKGALK KLIHAAKLNA SLKTLEGERN QIYIQLSEVD KTKEELTEHI
KSLQTEQASL QSENTHFENE NQKLQQKLKV MTELYQENEM KLHRKLTVEE NYRLEKEEKL
SKVDEKISHA TEELETYRKR AKDLEEELER TIHSYQGQII SHEKKAHDNW LAARNAERNL
NDLRKENAHN RQKLTETEFK FELLEKDPYA LDVPNTAFGR EHSPYGPSPL GRPSSETRAF
LSPPTLLEGP LRLSPLLPGG GGRGSRGPGN PLDHQITNER GESSCDRLTD PHRAPSDTGS
LSPPWEQDRR MMFPPPGQSY PDSALPPQRQ DRFFSNSGRL SGPAELRSFN MPSLDKMDGS
MPSEMESSRN DTKDDLGNLN VPDSSLPAEN EATGPGFVPP PLAPIRGPLF PVDTRGPFLR
RGPPFPAPPP GAMFGTSRDY FPPRDFPGPP HAPFAMRNVY PPRGFPPYLP PRPGFFPPPP
HSEGRSEFPS GLIPPSNEPA TEHPEPQQET
//
