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8DL8

Cryo-EM structure of human ferroportin/slc40 bound to Co2+ in nanodisc

Functional Information from GO Data
ChainGOidnamespacecontents
A0002260biological_processlymphocyte homeostasis
A0003158biological_processendothelium development
A0005381molecular_functioniron ion transmembrane transporter activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006366biological_processtranscription by RNA polymerase II
A0006826biological_processiron ion transport
A0006879biological_processintracellular iron ion homeostasis
A0006915biological_processapoptotic process
A0008021cellular_componentsynaptic vesicle
A0015093molecular_functionferrous iron transmembrane transporter activity
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0017046molecular_functionpeptide hormone binding
A0034755biological_processiron ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0043066biological_processnegative regulation of apoptotic process
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0048536biological_processspleen development
A0051649biological_processestablishment of localization in cell
A0055085biological_processtransmembrane transport
A0060345biological_processspleen trabecula formation
A0060586biological_processmulticellular organismal-level iron ion homeostasis
A1903988biological_processiron ion export across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
CTYR212-HIS218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues134
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:32814342
ChainResidueDetails
AMET1-SER23
ALYS85-ALA87
AALA163-GLY164
ATHR230-PRO306
ACYS367-GLY368
AVAL484-GLU488
AGLN543-VAL571

site_idSWS_FT_FI2
Number of Residues329
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:32814342, ECO:0007744|PDB:6W4S
ChainResidueDetails
AALA24-LEU53
ALEU58-ASP84
AARG88-HIS118
ATRP127-VAL162
AGLU165-ILE195
AILE203-LYS229
AVAL307-TYR333
AGLY339-LYS366
ALEU369-VAL391
ASER454-ASN483
AARG489-LEU513
APRO517-ALA542

site_idSWS_FT_FI3
Number of Residues83
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:32814342
ChainResidueDetails
ATYR54-SER57
AGLU119-GLY126
AMET196-VAL202
ATHR334-SER338
APHE392-ILE453
AALA514-ASN516

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:32814342
ChainResidueDetails
AASP39
AHIS43
ACYS326
AHIS507

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN434

221051

PDB entries from 2024-06-12

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